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AAA Biotech also known as AAA Bio or AAABio provides a variety of high-quality recombinant and natural/native proteins that are proven to work in a wide range of experiments. Explore our products to find the active protein that best fits your needs or experimental model.
Viewing 2000-2050 of 2583 product results
MERS-CoV S-trimer Protein, Active Protein (Cat# AAA177996)
Full Name
Recombinant MERS-CoV S-trimer Protein (R751S, C-6His)(Active)
Purity
>95% as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
(Recombinant SARS-CoV-2 Spike RBD Protein (C-His Tag)(Omicron))
COVID 19 Spike RBD Coronavirus, Active Protein (Cat# AAA177997)
Full Name
Recombinant SARS-CoV-2 Spike RBD Protein (C-His Tag)(Omicron)
Purity
>95% as determined by SDS-PAGE.
Pricing
Retinol-binding protein, Active Protein (Cat# AAA78134)
Full Name
Retinol-binding protein 4 (RBP4) from human plasma,
Gene Names
RBP4; RDCCAS
Purity
Affinity chromatography and size-exclusion chromatography
Pricing
Beta-Nerve Growth Factor (NGF), Active Protein (Cat# AAA235613)
Full Name
Recombinant Human Beta-nerve growth factor (NGF) (Active)
Gene Names
NGF; NGFB; HSAN5; Beta-NGF
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Interleukin-7 (IL7), Active Protein (Cat# AAA235615)
Full Name
Recombinant Human Interleukin-7 (IL7)
Gene Names
IL7; IL-7
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Interleukin-15 & Interleukin-15 Receptor Subunit alpha (IL15 & IL15RA), Active Protein (Cat# AAA235616)
Full Name
Recombinant Human Interleukin-15 & Interleukin-15 Receptor Subunit alpha (IL15 & IL15RA)
Gene Names
IL15RA; CD215
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Application Data
(Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in tau fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) over time in tau monomers. A greater increase in fluorescence is seen when 50 uM monomer is combined with 10 uM PFFs, as the fibrils seed the formation of new fibrils from the pool of monomers. Thioflavin T ex = 450 nm, em = 485 nm.)
Tau441, Active Protein (Cat# AAA253967)
Full Name
Active Human Recombinant Tau441 (2N4R), P301S Mutant Protein Monomer
Gene Names
MAPT; TAU; MSTD; PPND; DDPAC; MAPTL; MTBT1; MTBT2; FTDP-17; PPP1R103
Applications
Western Blot
Purity
>95%
Ion-Exchange Purified
Ion-Exchange Purified
Pricing
SDS_PAGE
(SDS-PAGE of ~15 kDa Active Human Tau Protein K18 P301L Preformed Fibrils. Lane 1: MW Ladder. Lane 2: Tau Protein Preformed Fibrils.)
Tau, Active Protein (Cat# AAA253968)
Full Name
Active Human Recombinant Tau (K18), P301L Mutant Protein Preformed Fibrils
Gene Names
MAPT; TAU; MSTD; PPND; DDPAC; MAPTL; MTBT1; MTBT2; FTDP-17; PPP1R103
Applications
Western Blot
Purity
>95%
Ion-Exchange Purified
Ion-Exchange Purified
Pricing
Bioactivity
(Fibroblast Growth Factor 12 (FGF12) is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. Fibroblast Growth Factor 12 (FGF12) may represent an important modulator of neuronal network activity and has been associated with developmental and epileptic encephalopathy (DEE). Besides, it is reported that both domains of (Ca2)4-CaM directly bind two sites in the N-terminal domain (NTD) of A-type FGF splice variants (FGF11A, FGF12A, FGF13A, and FGF14A) with high affinity. Calmodulin 1 (CALM1) has been identified as an interactor of FGF12, thus a binding ELISA assay was conducted to detect the interaction of recombinant human FGF12 and recombinant human CALM1. Briefly, FGF12 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CALM1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FGF12 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630nm immediately. The binding activity of recombinant human FGF12 and recombinant human CALM1 was shown in Figure 1, the EC50 for this effect is 4.44 ug/mL.)
Fibroblast Growth Factor 12 (FGF12), Active Protein (Cat# AAA161897)
Full Name
Active Fibroblast Growth Factor 12 (FGF12)
Gene Names
FGF12; FHF1; FGF12B
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Carbonic Anhydrase (CA) catalyzes the reversible reaction of CO2 H2O = HCO3- H, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. CA3 is a cytosolic enzyme with a very low CA activity. It is expressed at low levels in human muscle during early development but increases rapidly during the last trimester to reach 50-60% of adult levels at birth. The activity of recombinant human CA3 was measured by its ability to hydrolyze 4-Nitrophenyl acetate (4-NPA) to 4-Nitrophenol. The reaction was performed in 12.5 mM Tris, 75 mM NaCl, pH 7.5 (assay buffer), initiated by addition 50 uL of various concentrations of CA3 (diluted by assay buffer) to 50 uL of 2 mM substrate 4-NPA (100 mM stock in Acetone, diluted by assay buffer). Incubated at 37 degree C for 5min, then read at a wavelength of 400 nm.)
Carbonic Anhydrase III, Muscle Specific (CA3), Active Protein (Cat# AAA161899)
Full Name
Active Carbonic Anhydrase III, Muscle Specific (CA3)
Gene Names
CA3; Car3; CAIII
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Glypican 5 (GPC5) belongs to the glypican family of proteoglycans that are linked to the cell surface through a glycosyl-phosphatidylinositol anchor. GPC5 is expressed primarily in embryonic neurons and mesenchyme and it is implicated in a variety of physiological processes, ranging from cell proliferation to morphogenesis. Besides, Syndecan 1 (SDC1) has been identified as an interactor of GPC5, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat GPC5 and recombinant human SDC1. Briefly, GPC5 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to SDC1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GPC5 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant rat GPC5 and recombinant human SDC1 was shown in Figure 1, the EC50 for this effect is 0.6 ug/mL.)
Glypican 5 (GPC5), Active Protein (Cat# AAA161913)
Full Name
Active Glypican 5 (GPC5)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Ephrin-A1 (EFNA1), also known as EPLG1, LERK1, TNFAIP4, Immediate early response protein B61, is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. EFNA1 plays an important role in angiogenesis and tumor neovascularization. EFNA1 widely affects tumor growth through enhancing tumor angiogenesis, malignant cell events and invasiveness. Ephrin Type A Receptor 1 (EPHA1) is one of high-affinity ligands for EFNA1, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human EFNA1 and recombinant mouse EPHA1. Briefly, biotin-linked EFNA1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to EPHA1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of recombinant human EFNA1 and recombinant mouse EPHA1 was shown in Figure 1, the EC50 for this effect is 0.24 ug/mL.)
Ephrin A1 (EFNA1), Active Protein (Cat# AAA161914)
Full Name
Active Ephrin A1 (EFNA1)
Gene Names
EFNA1; B61; EFL1; ECKLG; EPLG1; LERK1; LERK-1; TNFAIP4
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Ephrin A2 (EFNA2) is a cell surface-associated protein belonging to the Ephrin family, which are involved in intercellular communication and cell localization. EFNA2 is mainly expressed in tissues including the brain, heart, lung, kidney and pancreas. And this protein is involved in regulating a variety of biological processes, including cell migration, cell differentiation, and tissue boundary formation, by interacting with Eph receptors. It aslo plays a significant role in the development and maintenance of the cardiovascular system, as well as in the regulation of synaptic plasticity and neuronal circuitry in the brain. A Disintegrin And Metalloprotease 10 (ADAM10), a disintegrin and metalloproteinase, can cleave EFNA2, potentially altering the activity of EFNA2 or its interaction with Eph receptors, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human EFNA2 and recombinant rat ADAM10. Briefly, biotin-linked EFNA2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to ADAM10-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of EFNA2 and ADAM10 was shown in Figure 1, the EC50 for this effect is 1.38 ug/mL.)
Ephrin A2 (EFNA2), Active Protein (Cat# AAA161915)
Full Name
Active Ephrin A2 (EFNA2)
Gene Names
EFNA2; ELF-1; EPLG6; LERK6; HEK7-L; LERK-6
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Ephrin-A4, also known as EFNA4 and EFL-4, is a member of the ligand of the EPH family. It is mainly expressed in the spleen, lymph nodes, ovary, small intestine and colon of adults, as well as in the heart, lungs, liver, and kidneys of the fetus. It is involved in the development of neurons, blood vessels, and epithelium by regulating cell migration, rejection, and adhesion. Ephrin-A4 has been shown to bind FYN,EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat EFNA4 and recombinant human FYN. Briefly, EFNA4 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FYN-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-EFNA4 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant rat EFNA4 and recombinant human FYN was shown in Figure 1, the EC50 for this effect is 0.37 ug/mL.)
Ephrin A4 (EFNA4), Active Protein (Cat# AAA161918)
Full Name
Active Ephrin A4 (EFNA4)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(To test the effect of MIA1 on cell apoptosis, A375 cells were seeded into triplicate wells of 96-well plates at a density of 4,000 cells/well and allowed to attach overnight, then the medium was replaced with various concentrations of recombinant human MIA1 diluted with 5% serum standard DMEM. After incubated for 48h, cells were observed by inverted microscope and cell viability was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then the absorbance at 450 nm was measured using a microplate reader after incubating the plate for 1-4 hours at 37 degree C. Apoptosis of A375 cells after incubation with MIA1 for 48h observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 assay after incubation with recombinant human MIA1 for 48h. The result was shown in Figure 2. It was obvious that MIA1 significantly decreased cell viability of A375 cells. The ED50 of recombinant human MIA1 is 0.53 ug/ml.)
Melanoma Inhibitory Activity Protein 1 (MIA1), Active Protein (Cat# AAA161926)
Full Name
Active Melanoma Inhibitory Activity Protein 1 (MIA1)
Gene Names
MIA; CD-RAP
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Cystatin D is a member of family 2 of the cystatin superfamily. In contrast to other members of family 2, Cystatin D has restricted tissue distribution and has been found only in saliva and tears. Two allelic variants (Arg46 and Cys46) are known in the human protein and they are not significantly different in their inhibitory activity against papain and cathepsins B, H, L and S. Recombinant Human Cystatin D corresponds to the Arg46 variant. The functions of Cystatin D are largely unknown. However, Cystatin D has been shown to inhibit coronavirus replication at its physiological concentration (0.121.9 uM) and has been suggested to play a protective role against proteases present in the oral cavity. The activity of recombinant human Cystatin D was measured by its ability to inhibit papain cleavage of a fluorogenic peptide substrate Z-FR-AMC in the assay buffer 50 mM Tris, pH 7.0. Papain was diluted to 500 ug/ml in activation buffer 50 mM Tris, 5 mM DTT, pH 7.0 and incubated at room temperature for 15 minutes. The activated papain was diluted to 100 ug/ml in the assay buffer and 20 ul different concentrations of recombinant human Cystatin D (MW: 17.45 KD) was incubated with 20 ul 100 ug/ml papain at 37 degree C for 10 minutes. Loading 50 uL of the incubated mixtures which were diluted five-fold in assay buffer into empty wells of a plate, and start the reaction by adding 50 uL of 200 uM substrate. Include a substrate blank containing 50 uL of assay buffer and 50 uL of 200 uM substrate. Then read at excitiation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant human Cystatin D significantly decreased papain activity. The inhibition IC50 was )
Cystatin 5 (CST5), Active Protein (Cat# AAA161930)
Full Name
Active Cystatin 5 (CST5)
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Sequence
Steroid 5 Alpha Reductase 1 (SRD5a1), Active Protein (Cat# AAA161940)
Full Name
Active Steroid 5 Alpha Reductase 1 (SRD5a1)
Gene Names
Srd5a1; S5AR 1; Srd5a-1; 0610031P22Rik; 4930435F02Rik
Applications
Activity Assay
Purity
>80%
Pricing
Bioactivity
(Human TFPI, also known as lipoprotein-associated coagulation inhibitor (LACI) and extrinsic pathway inhibitor (EPI), is a physiological inhibitor of extrinsic pathway of coagulation and has biological functions of anticoagulation and anti-inflammation. It is a secreted protein with a N-terminal acidic region, three Kunitz (K) domains separated with by two linker regions, and a C-terminal basic region. The activity of recombinant human TFPI was measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate Mca-RPKPVE-Nval-WRK(Dnp)-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. Trypsin was diluted to 50 ug/ml in the assay buffer and 20 ul different concentrations of recombinant human TFPI (MW: 55.58 KD) was incubated with 20 ul diluted trypsin at 37 degree C for 15 minutes. Loading 50 uL of the incubated mixtures which were diluted five-fold in assay buffer into empty wells of a plate, and start the reaction by adding 50 uL of 20 uM substrate. Include a substrate blank containing 50 uL of assay buffer and 50 uL of 20 uM substrate. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant human TFPI significantly decreased trypsin activity. The inhibition IC50 was )
Tissue Factor Pathway Inhibitor (TFPI), Active Protein (Cat# AAA161731)
Full Name
Active Tissue Factor Pathway Inhibitor (TFPI)
Gene Names
TFPI; EPI; TFI; LACI; TFPI1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
SDS-PAGE
(Sample: Active recombinant EMILIN1, Human)
Elastin Microfibril Interface Located Protein 1 (EMILIN1), Active Protein (Cat# AAA161733)
Full Name
Active Elastin Microfibril Interface Located Protein 1 (EMILIN1)
Gene Names
EMILIN1; EMI; gp115; EMILIN
Reactivity
Homo sapiens (Human)
Applications
Activity Assay
Purity
>80%
Pricing
Bioactivity
(Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha) is also a component of Follicle-Stimulating Hormone (FSH), Thyroid-Stimulating Hormone, and Chorionic Gonadotropin. The unique beta subunit confers the protein's specific biological action and is responsible for the interaction with its receptor. LH is produced and secreted by the anterior pituitary gland. Its secretion is controlled by Gonadotropin-Releasing Hormone from the hypothalamus; however, LH secretion can also be stimulated by estradiol. A functional binding ELISA assay was conducted to detect the interaction of recombinant human CGa/LHb and recombinant human Dopamine Receptor D1 (DRD1). Briefly, biotin-linked CGa/LHb were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to DRD1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of CGa/LHb and DRD1 was shown in Figure 1, the EC50 for this effect is 0.644 ug/mL.)
Luteinizing Hormone (LH), Active Protein (Cat# AAA161734)
Full Name
Active Luteinizing Hormone (LH)
Gene Names
CGA; HCG; LHA; FSHA; GPHa; TSHA; GPHA1; CG-ALPHA
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Serpin B2, also known as PAI-2, is an approximately 60 kDa serine protease inhibitor. It is primarily secreted by macrophages and monocytes and can form disulfide-linked multimers. Serpin B2 inhibits both the urokinase-type and tissue-type plasminogen activators (uPA and tPA). Serpin B2 also promotes the clearance of uPA by enhancing its binding and uptake by LRP. It limits fibril formation by Huntington protein (HTT) and beta-Amyloid peptides. It promotes Th2 biased immune responses and is important for intestinal CCL2 production, monocyte recruitment, and nematode clearance. A non-glycosylated form of Serpin B2 is retained intracellularly where it interferes with TNF-a induced apoptosis by protecting the Retinoblastoma protein (RB1) from calpain digestion. It also inhibits proteasome activity in activated endothelial cells. The activity of recombinant mouse PAI-2 was measured by its ability to inhibit uPA cleavage of a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC) in the assay buffer 50 mM Tris, 0.01% Tween 20, pH 8.5. The 50 ul different concentrations of rmPAI-2 (MW: 47.9 KD) was incubated with 50ul 2ug/ml rhuPA (EPA140Mu61) at room temperature for 15 minutes. Loading 50 uL of the incubated mixtures into empty wells of a plate, and start the reaction by adding 50 uL of 200 uM substrate (Z-GGR-AMC). Include a substrate blank containing 50 uL of assay buffer and 50 uL of 200 uM substrate. Then read at excitiation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that PAI2 significantly decreased uPA activity. The inhibition IC50 was )
Plasminogen Activator Inhibitor 2 (PAI2), Active Protein (Cat# AAA161740)
Full Name
Active Plasminogen Activator Inhibitor 2 (PAI2)
Gene Names
Serpinb2; PAI-2; Planh2; ovalbumin
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Tissue inhibitors of metalloproteinase 1 (TIMP1) is a member of the family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). TIMP-1 is a glycoprotein with a molecular mass of 28 kDa produced by a wide range of cell types. TIMP-1 inhibits active MMP-mediated proteolysis by forming an N-terminal, non-covalent binary complex with the MMP active site. The activity of recombinant dog TIMP1 was measured by its ability to inhibit rhMMP2 cleavage of a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. rhMMP2 was diluted to 100 ug/ml and activated with 1 mM APMA at 37 degree C for 1 hour and TIMP1 (MW: 20.86 KD) was diluted to different concentrations with the assay buffer. Mix 8 ul of TIMP1 curve dilutions, 12.8 ul of activated rhMMP-2, and 59.2 ul of assay buffer, including a control containing assay buffer and the diluted rhMMP-2 and incubate the reactions for 2 hours at 37 degree C. Loading 50 ul of the incubated mixtures which were diluted five-fold in assay buffer into empty wells of a plate, and start the reaction by adding 50 ul of 20 uM substrate. Include a substrate blank containing 50 ul of assay buffer and 50 ul of 20 uM substrate. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant dog TIMP1 significantly decreased rhMMP2 activity. The inhibition IC50 was )
Tissue Inhibitors Of Metalloproteinase 1 (TIMP1), Active Protein (Cat# AAA161742)
Full Name
Active Tissue Inhibitors Of Metalloproteinase 1 (TIMP1)
Gene Names
TIMP1; TIMP-1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. The activity of recombinant human MMP9 is measured by its ability to cleave a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rhMMP9 is diluted to 100 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 degree C for 1 hours. The activated rhMMP9 is diluted to 0.2 ug/mL in assay buffer. Loading into a black well plate 50 uL of 0.2 ug/mL rhMMP9 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhMMP9. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human MMP9 is > 3000 pmol/min/ug.)
Matrix Metalloproteinase 9 (MMP9), Active Protein (Cat# AAA161746)
Full Name
Active Matrix Metalloproteinase 9 (MMP9)
Gene Names
MMP9; GELB; CLG4B; MMP-9; MANDP2
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Homing Associated Cell Adhesion Molecule (HCAM), also known as CD44, is a ubiquitous multistructural and multifunctional cells surface adhesion molecule involved in cell-cell and cell-matrix interactions. CD44 is broadly expressed, including in the membranes of B cells, granulocytes, monocytes, and erythrocytes as well as on many thymocytes and mature T cells, besides it is highly expressed in many cancers and regulates metastasis via recruitment of CD44 to the cell surface. This protein is a receptor for hyaluronic acid (HA) and can also interact with other ligands, such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse HCAM and biotinylated hyaluronan (HA). Briefly, biotin-linked HA was diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to HCAM-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 1 hour, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant mouse HCAM and biotinylated HA was shown in Figure 1, and this effect was in a dose dependent manner.)
Homing Associated Cell Adhesion Molecule (HCAM), Active Protein (Cat# AAA161764)
Full Name
Active Homing Associated Cell Adhesion Molecule (HCAM)
Gene Names
Cd44; Ly-24; Pgp-1; HERMES; AU023126; AW121933; AW146109
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Tissue kallikreins are a family of extracellular serine proteases consisting of 15 members. Tissue kallikreins have attracted great interest as potential biomarkers for various cancers, including prostate, ovarian, breast, testicular, and lung. Human Kallikrein 6 (hKLK6) is a member of tissue kallikrein family observed in breast and brain tissues, colon carcinoma cells, and oligodedrocytes. Known protein substrates of hKLK6 are myelin basic protein, the precursor of the A beta amyloid peptide, and plasminogen. Its physiological functions may include the participation in demyelination processes as well as in the progression of inflammatory disease of the CNS. The activity assay of recombinant mouse KLK6 was measured by its ability to cleave the fluorogenic peptide substrate Boc-QAR-AMC. The rmKLK6 was activated by Lysyl-endopeptidase in the activation buffer 50 mM Tris, 0.05% (w/v) Brij-35, pH 8.0, of which equal volumes of 200 ug/ml rmKLK6 and 2.5 mU/ml Lysyl-endopeptidase were combined and incubated at room temperature for 30 minutes. The activated rmKLK6 was diluted to 3 ug/ml in assay buffer and start the reaction by adding 50 uL of 200 uM substrate. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes. The specific activity of recombinant mouse KLK6 is >6000 pmol/min/ug.)
Kallikrein 6 (KLK6), Active Protein (Cat# AAA161769)
Full Name
Active Kallikrein 6 (KLK6)
Gene Names
Klk6; BSP; MSP; Bssp; Klk29; Prss9; Prss18; AI849898; neurosin
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(C reactive protein (CRP) is an annular (ring-shaped), pentameric protein found in blood plasma, whose levels rise in response to inflammation. It is an acute-phase protein of hepatic origin that increases following interleukin-6 secretion by macrophages and T cells. Its physiological role is to bind to lysophosphatidylcholine expressed on the surface of dead or dying cells (and some types of bacteria) in order to activate the complement system via C1q. Besides, Coagulation Factor II (F2) has been identified as an interactor of CRP, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant dog CRP and recombinant rat F2. Briefly, CRP was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to F2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CRP pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant dog CRP and recombinant rat F2 was shown in Figure 1, the EC50 for this effect is 0.82 ug/mL.)
C ReProtein (CRP), Active Protein (Cat# AAA161778)
Full Name
Active C Reactive Protein (CRP)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(PRL (prolactin), also known as luteotropin, is a hormone secreted from the pituitary gland and is best known for its role in enabling mammals to produce milk. PRL plays an essential role in metabolism, regulation of the immune system through activating its specific membrane-anchored receptor (PRLR). A functional ELISA assay was conducted to detect the interaction of recombinant bovine PRL and recombinant human PRLR. Briefly, PRL was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PRLR-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PRL pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant bovine PRL and recombinant human PRLR was shown in Figure 1, the EC50 for this effect is 0.05 ug/mL.)
Prolactin (PRL), Active Protein (Cat# AAA161787)
Full Name
Active Prolactin (PRL)
Gene Names
PRL; GHA1; Prol
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(PRL (prolactin), also known as luteotropin, is a hormone secreted from the pituitary gland and is best known for its role in enabling mammals to produce milk. PRL plays an essential role in metabolism, regulation of the immune system through activating its specific membrane-anchored receptor (PRLR). A functional binding ELISA assay was conducted to detect the interaction of recombinant horse PRL and recombinant human PRLR. Briefly, PRL was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PRLR-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PRL pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant horse PRL and recombinant human PRLR was shown in Figure 1, the EC50 for this effect is 0.11 ug/mL.)
Prolactin (PRL), Active Protein (Cat# AAA161789)
Full Name
Active Prolactin (PRL)
Gene Names
PRL; GHA1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Carbonic Anhydrase (CA) catalyzes the reversible reaction of CO2 H2O = HCO3- H, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. CA1 is a cytosolic enzyme with the highest levels in erythrocytes and is a very early marker for erythroid differentiation. The activity of recombinant human CA1 was measured by its ability to hydrolyze 4-Nitrophenyl acetate (4-NPA) to 4-Nitrophenol. The reaction was performed in 12.5 mM Tris, 75 mM NaCl, pH 7.5 (assay buffer), initiated by addition 50 uL of various concentrations of CA1 (diluted by assay buffer) to 50 uL of 2 mM substrate 4-NPA (100 mM stock in Acetone, diluted by assay buffer). Incubated at 37 degree C for 5min, then read at a wavelength of 400 nm.)
Carbonic Anhydrase I (CA1), Active Protein (Cat# AAA161796)
Full Name
Active Carbonic Anhydrase I (CA1)
Gene Names
CA1; CAB; CA-I; Car1
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Peroxisome Proliferator Activated Receptor Gamma (PPARg) belongs to a large group of nuclear receptors controlling reproduction, metabolism, development and immune response. It is mainly expressed in adipose tissue, hematopoietic cells and the large intestine and it plays an important role in adipocyte differentiation, lipid and glucose metabolism, and modulation of immune and inflammatory reactions. Besides, Peroxisome Proliferator Activated Receptor Gamma Coactivator 1 Alpha (PPARgC1a) has been identified as an interactor of PPARg, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human PPARg and recombinant mouse PPARgC1a. Briefly, PPARg was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PPARgC1a-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PPARg pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human PPARg and recombinant mouse PPARgC1a was shown in Figure 1, the EC50 for this effect is 0.03 ug/mL.)
Peroxisome Proliferator Activated Receptor Gamma (PPARg), Active Protein (Cat# AAA161802)
Full Name
Active Peroxisome Proliferator Activated Receptor Gamma (PPARg)
Gene Names
PPARG; GLM1; CIMT1; NR1C3; PPARG1; PPARG2; PPARgamma
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Figure 2. Inhibition of HepG2 cells proliferation after stimulated with recombinant rat BMP4)
Bone Morphogenetic Protein 4 (BMP4), Active Protein (Cat# AAA161655)
Full Name
Active Bone Morphogenetic Protein 4 (BMP4)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Fibroblast Growth Factor 9 (FGF9) is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. FGF9 secreted by HSC is a candidate activating ligand for hepatocyte FGFR4 functions, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human FGF9 and recombinant human FGFR4. Briefly, biotin-linked FGF9 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FGFR4-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30 min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of FGF9 and FGFR4 was shown in Figure 1, the EC50 for this effect is 0.23 ug/mL.)
Fibroblast Growth Factor 9 (FGF9), Active Protein (Cat# AAA161661)
Full Name
Active Fibroblast Growth Factor 9 (FGF9)
Gene Names
FGF9; GAF; FGF-9; SYNS3; HBFG-9; HBGF-9
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Growth Hormone (GH), also known as somatotropin, is a member of a family of growth factors. Human growth hormone is a 191 amino acid single-chain polypeptide produced via the anterior pituitary of the brain in the acidophilic, somatotrophic cells. Its production is tightly regulated through several complex feedback mechanisms in response to stress, exercise, nutrition, sleep, and growth hormone itself. Annexin A2 (ANXA2) has been shown to play multiple roles in growth, development, metabolism and ANXA2 is a high affinity receptor for GH. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human GH and recombinant human ANXA2. Briefly, GH was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to ANXA2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GH pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human GH and recombinant human ANXA2 was shown in Figure 1, the EC50 for this effect is 2.1 ug/mL.)
Growth Hormone (GH), Active Protein (Cat# AAA161667)
Full Name
Active Growth Hormone (GH)
Gene Names
GH1; GH; GHN; GH-N; hGH-N; IGHD1B
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Insulin-like growth factor-binding protein 3, also known as IGFBP3 is one of sixIGF binding proteins (IGFBP1 to IGFBP6) that have highly conserved structuresand bind the insulin-like growth factors IGF-1 and IGF-2 with high affinity. Withintissues, IGFBP3 can bind IGF1 and IGF2 released by many cell types, and blocktheir access to the IGF-1 receptor (IGF1R), which is activated by both IGFs.IGFBP3 also interacts with cell-surface proteins, affecting cell signaling fromoutside the cell or after internalization, and also enters the cell nucleus where itbinds to nuclear hormone receptors and other ligands. Besides, Fibronectin (FN)has been identified as an interactor of IGFBP3, thus a binding ELISA assay wasconducted to detect the interaction of recombinant human IGFBP3 andrecombinant human FN.Briefly, IGFBP3 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicatesamples of 100ul were then transferred to FN-coated microtiter wells andincubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1hwith anti-IGFBP3 pAb, then aspirated and washed 3 times. After incubation withHRP labelled secondary antibody, wells were aspirated and washed 5 times.With the addition of substrate solution, wells were incubated 15-25 minutes at37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately.The binding activity of IGFBP3 and FN was shown in Figure 1, the EC50 was 78ng/ml.)
Insulin Like Growth Factor Binding Protein 3 (IGFBP3), Active Protein (Cat# AAA161673)
Full Name
Active Insulin Like Growth Factor Binding Protein 3 (IGFBP3)
Gene Names
IGFBP3; IBP3; BP-53
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Interleukin 1 alpha (IL-1alpha) also known as hematopoietin 1 is a cytokine of the interleukin 1 family that in humans is encoded by the IL1A gene. IL-1alphais produced mainly by activated macrophages, as well as neutrophils, epithelial cells, and endothelial cells. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. To test the effect of IL-1alpha on cell apoptosis, MCF7 cells were seeded into 96-well plates at a density of 4,000 cells/well with 5% serum standard DMEM including various concentrations of recombinant goat IL-1alpha. After incubated for 72h, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then the absorbance at 450 nm was measured using a microplate reader after incubating the plate for 1-2 hours at 37 degree C. Proliferation of MCF7 cells after incubation with IL-1alpha for 72h observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 (Cell Counting Kit-8) assay after incubation with recombinant goat IL-1alpha for 72h. The result was shown in Figure 2. It was obvious that IL-1alpha significantly inhibit cell viability of MCF7cells. The ED50 is 2.13 ug/ml.)
Interleukin 1 Alpha (IL1a), Active Protein (Cat# AAA161676)
Full Name
Active Interleukin 1 Alpha (IL1a)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(IL1alpha(Interleukin-1 alpha) is a member of the interleukin 1 cytokine family. This cytokine is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces cell apoptosis. It is reported that exposure of MCF-7 cells to certain concentration of IL1alpha results in inhibition of cell growth. Thus, an cell proliferation assay of MCF-7 was conducted with the addition of IL1alpha. MCF-7 cells were seeded overnight at a density of 4,000 cells/well, and then treated with or without various concentrations of IL1alpha for 72h, then cells were observed by inverted microscope and cell viability was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then measure the absorbance at 450 nm using a microplate reader after incubating the plate for 1-4 hours in at 37 degree C. Inhibition of MCF-7 cell proliferation after incubation with IL1alpha for 72h observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 (Cell Counting Kit-8) assay after incubation with various concentrations of IL1alpha for 72h. The mean OD value of MCF-7 assessed by CCK-8 was shown in Figure 2. It was obvious that IL1alpha significantly decreased cell viability of MCF-7 cells and the EC50 was 4.69 ug/ml.)
Interleukin 1 Alpha (IL1a), Active Protein (Cat# AAA161677)
Full Name
Active Interleukin 1 Alpha (IL1a)
Gene Names
IL1A; IL1; IL-1A; IL1F1; IL1-ALPHA
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Interleukin-5 (IL-5), a secreted glycoprotein, is a member of the hematopoietic family. Interleukin 5 has been shown to stimulate the proliferation of TF-1 cells. To test this effect, TF-1 cells were seeded into triplicate wells of 96-well plates at a density of 2 x 104 cells/well and incubated for 72h in the presence or absence of various concentrations of recombinant human IL-5 at 37 degree C. The growth of cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then measure the absorbance at 450 nm using a microplate reader after incubating the plate for 1-4 hours at 37 degree C. Cell proliferation of TF-1 cells after incubation with IL-5 for 72h observed by inverted microscope was shown in Figure 1. The dose-effect curve of recombinant human IL-5 was shown in Figure 2. It was obvious that it significantly promoted cell proliferation of TF-1 cells. The ED50 for this effect is typically 35 ng/ml.)
Interleukin 5 (IL5), Active Protein (Cat# AAA161678)
Full Name
Active Interleukin 5 (IL5)
Gene Names
IL5; EDF; TRF; IL-5
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Leukemia inhibitory factor (LIF), is an interleukin 6 class cytokine that affects cell growth by inhibiting differentiation. LIF as a cytokine also has another fuction including: the growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation. The activity of LIF is usually measured by a cell proliferation assay using TF-1 cells. TF-1 cells were seeded into triplicate wells of 96-well plates at a density of 20000 cells/well with 10% serum standard 1640 which contains various concentrations of recombinant human LIF. After incubated for 3 days, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then the absorbance at 450 nm was measured using a microplate reader after incubating the plate for 2-4 hours at 37 degree C. Proliferation of TF-1 cells after incubation with LIF for 3 days observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 (Cell Counting Kit-8) assay after incubation with rhLIF for 3 days. The result was shown in Figure 2. It was obvious that rhLIF significantly increased cell viability of TF-1 cells. The ED50 is 1.86 ng/ml.)
Leukemia Inhibitory Factor (LIF), Active Protein (Cat# AAA161682)
Full Name
Active Leukemia Inhibitory Factor (LIF)
Gene Names
LIF; CDF; DIA; HILDA; MLPLI
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(MMP1 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin and so on. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain. The activity of recombinant bovine MMP1 is measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rbMMP1 is diluted to 50 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 degree C for 2 hours. The activated rbMMP-1 is diluted to 1 ug/mL in assay buffer. Loading into a black well plate 50 uL of 1 ug/mL rbMMP-1 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rbMMP-1. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant bovine MMP1 is > 150 pmol/min/ug.)
Matrix Metalloproteinase 1 (MMP1), Active Protein (Cat# AAA161684)
Full Name
Active Matrix Metalloproteinase 1 (MMP1)
Gene Names
MMP1; MMP-1
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(MMP1 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin and so on. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain. The activity of recombinant sheep MMP1 is measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rsMMP1 is diluted to 50 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 degree C for 2 hours. The activated rsMMP-1 is diluted to 1 ug/mL in assay buffer. Loading into a black well plate 50 uL of 1 ug/mL rsMMP-1 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rsMMP-1. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant sheep MMP1 is > 40 pmol/min/ug.)
Matrix Metalloproteinase 1 (MMP1), Active Protein (Cat# AAA161685)
Full Name
Active Matrix Metalloproteinase 1 (MMP1)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(MMP1 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin and so on. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain. The activity of recombinant pig MMP1 is measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rpMMP1 is diluted to 50 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 degree C for 2 hours. The activated rpMMP-1 is diluted to 1 ug/mL in assay buffer. Loading into a black well plate 50 uL of 1 ug/mL rpMMP-1 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rpMMP-1. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant pig MMP1 is > 10 pmol/min/ug.)
Matrix Metalloproteinase 1 (MMP1), Active Protein (Cat# AAA161686)
Full Name
Active Matrix Metalloproteinase 1 (MMP1)
Gene Names
MMP1; Mmp1a
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Figure 2. Cell proliferation of TF-1 cells after stimulated with recombinant human NGF.)
Nerve Growth Factor (NGF), Active Protein (Cat# AAA161688)
Full Name
Active Nerve Growth Factor (NGF)
Gene Names
NGF; NGFB; HSAN5; Beta-NGF
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Glypican-3 (GPC3), a 70 kDa protein, is a member of the glypican family that attaches to the cell surface by a glycosylphosphatidylinositol anchor, is specifically up-regulated in hepatocellular carcinoma (HCC) although rarely or not expressed in normal liver tissues, making it a perfect test and treatment target for HCC. GPC3 is also a negative transcriptional regulator and tumor suppressor that inhibits the growth of breast, ovary, and lung cancer cells. It is reported that GPC3 can form a complex with insulin-like growth factor 2 (IGF2), and might thereby modulate IGF2 action. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human GPC3 and recombinant rat IGF2. Briefly, GPC3 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to IGF2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GPC3 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human GPC3 and recombinant rat IGF2 was shown in Figure 1, the EC50 for this effect is 0.08 ug/mL.)
Glypican 3 (GPC3), Active Protein (Cat# AAA161814)
Full Name
Active Glypican 3 (GPC3)
Gene Names
GPC3; SGB; DGSX; MXR7; SDYS; SGBS; OCI-5; SGBS1; GTR2-2
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(The cytochrome P450 enzyme CYP2E1 catalyzes the oxidative metabolism of many solvents and other small organic molecules. CYP2E1 is expressed in adult and fetal human liver in addition to extrahepatic tissues such as lung and placenta. Treatment of primary cultures of human hepatocytes with ethanol induces CYP2E1 protein, and this is consistent with the finding that hepatic CYP2E1 protein and mRNA levels are increased in individuals with alcoholism. Although only a few drugs (e.g., acetaminophen have been identified as substrates for CYP2E1, many low molecular weight procarcinogens are activated by this cytochrome P450 (P450). Chlorzoxazone 6-hydroxylation, N-nitrosodimethylamine N-demethylation and p-nitrophenol hydroxylation can be used to measure the catalytic activity of CYP2E1. Thus, the recombinant mouse CYP2E1 activity was measured by its ability to hydroxylate p-nitrophenol to p-nitrocatechol. The reaction was performed in 50 mM potassium phosphate, pH 7.4 (Assay Buffer), initiated by addition 20 uL of 500 ug/ml CYP2E1 to 10 uL of 5 mM substrate p-nitrophenol and 30 ul of 26 mM NADPH in a total volume of 500 ul. Incubated at 37 degree C for 30min, then read at a wavelength of 535 nm after acidification of the reaction mixture with trichloroacetic acid followed by neutralization using 2 M NaOH.)
Cytochrome P450 2E1 (CYP2E1), Active Protein (Cat# AAA161819)
Full Name
Active Cytochrome P450 2E1 (CYP2E1)
Gene Names
Cyp2e1; Cyp2e
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Tryptase is a serine protease with trypsin-like activity, which is sometimes also referred to as Mast Cell Protease 7. It is stored in the secretory granules of mouse mast cells. It exhibits anticoagulant activity due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma. The activity of recombinant human TPS is measured by its ability to cleave a fluorogenic peptide substrate Mca-Arg-Pro-Lys-Pro-Val-Glu-Nval-Trp-Arg-Lys(Dnp)-NH2 in the assay buffer 50 mM Tris, pH 8.5. The rhTPS is diluted to 200 ug/ml in 50 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.05% (w/v) Brij-35, pH 7.5, then activated with 0.1 ug/ml Thermolysin at 37 degree C for 15min followed by adding 10 mM 1, 10 phenanthroline to stop activation. The activated rhTPS is diluted to 50 ug/mL in heparin incubation buffer of 100 ug/mL heparin, 50 mM MES, pH 5.5 and incubated at room temperature for 2 hours. Then the rhTPS was diluted to 12.5 ug/ml in assay buffer and load into a black well plate 50 uL and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhTPS. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human TPS is > 25 pmol/min/ug.)
Tryptase (TPS), Active Protein (Cat# AAA161828)
Full Name
Active Tryptase (TPS)
Gene Names
TPSAB1; TPS1; TPS2; TPSB1
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Complement Component 4b (C4b) is a component of the complement system, which is activated by the recognition of foreign pathogens, such as bacteria and viruses, or altered self-cells. In the classical activation pathway of complement, C4b is produced by the proteolytic cleavage of the precursor protein C4 by the activated enzyme C1s, and it can bind to C2a to form C3 invertase (C4b2a) which is responsible for the cleavage of C3. Besides, the binding of MASP2 to C4b is an important step in the lectin pathway of the complement system, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human C4b and recombinant human MASP2. Briefly, C4b was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to MASP2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-C4b pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human C4b and recombinant human MASP2 was shown in Figure 1, the EC50 for this effect is 1.39 ug/mL.)
Complement C4-B (C4B), Active Protein (Cat# AAA161839)
Full Name
Active Complement C4-B (C4B)
Gene Names
C4B; CH; C4F; CO4; C4B1; C4B2; C4B3; C4B5; C4BD; C4B12; C4B_2; CPAMD3
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Thymic stromal lymphopoietin (TSLP) is a member of the IL-2 cytokine family and a distant paralog of IL-7. TSLP is a pleiotropic cytokine that acts on multiple cell lineages, including dendritic cells, T cells, B cells, neutrophils, mast cells, eosinophils and innate lymphoid cells, affecting their maturation, survival and recruitment. It is best known for its role in promoting type 2 immune responses such as in allergic diseases. Interleukin 13 (IL13) is a critical downstream element for TSLP-driven allergic inflammation. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human TSLP and recombinant bovine IL13. Briefly, TSLP was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to IL13-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-TSLP pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human TSLP and recombinant bovine IL13 was shown in Figure 1, the EC50 for this effect is 0.11 ug/mL.)
Thymic Stromal Lymphopoietin (TSLP), Active Protein (Cat# AAA161842)
Full Name
Active Thymic Stromal Lymphopoietin (TSLP)
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Hemoglobin (HB) is a protein in red blood cells which contains iron. It is used to transport oxygen around the human body. Hemoglobin is found in the red blood cells of almost all vertebrates. Hemoglobin has peroxidase activity. In the presence of hydrogen peroxide, hemoglobin can catalyze the substrates 3,3 ', 5,5' - tetramethylbenzidine (TMB) to produce a blue compound which has a maximum absorption at 595 nm. Thus, the activity of native chinese hamster hemoglobin was measured by its ability to catalyze the substrates of TMB. The reaction was performed in PBS, pH 7.4 (Assay Buffer), ainitiated by addition 40 uL of various concentrations of HB (diluted by Assay Buffer) to 160 uL of TMB. Incubated at 37 degree C for 20min, then read at a wavelength of 595 nm immediately. The result was shown in figure 1, and the OD value was in a linear relationship with the concentration of HB.)
Hemoglobin (HB), Active Protein (Cat# AAA161849)
Full Name
Active Hemoglobin (HB)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Complement Component 5 (C5), which forms part of the later stages of the complement pathway, is cleaved into C5a and C5b. C5a is a chemotactic agent for neutrophils, while C5b forms part of the complement membrane attack complex. Coagulation Factor II (F2) has been identified as an interactor of C5, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human C5 and recombinant mouse F2. Briefly, C5 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to F2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-C5 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human C5 and recombinant mouse F2 was shown in Figure 1, the EC50 for this effect is 0.22 ug/mL.)
Complement Component 5 (C5), Active Protein (Cat# AAA161871)
Full Name
Active Complement Component 5 (C5)
Gene Names
C5; C5a; C5b; CPAMD4
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Protein Z-dependent Protease Inhibitor (ZPI), also known as SerpinA10 (SERine Proteinase INhibitor-clade A10) is a monomeric, secreted member of the A (or extracellular) clade within the serpin superfamily of protease inhibitors. In general, members of this superfamily regulate multiple proteolytic cascades, and are particularly effective due to the fact that their inhibitory activities can be fine-tuned through the participation of discrete, non-serpin co-factors. Serpins are unusual in that they are one-time use, non-recyclable proteins whose native state is thermodynamically unstable. The activity of recombinant human SERPINA10 was measured by its ability to inhibit Coagulation Factor X cleavage of a fluorogenic peptide substrate Mca-RPKPVE-Nval-WRK(Dnp)-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. Coagulation Factor X was diluted to 5 ug/ml in the assay buffer and 25 ul different concentrations of recombinant human SERPINA10 (MW: 78.26 KD) was incubated with 25 ul diluted Coagulation Factor X at 37 degree C for 30 minutes. Loading 50 uL 20 uM substrate to start the reaction including a substrate blank containing 50 uL of assay buffer and 50 uL of 20 uM substrate. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant human SERPINA10 significantly decreased Coagulation Factor X activity. The inhibition IC50 was )
Serpin A10 (SERPINA10), Active Protein (Cat# AAA161873)
Full Name
Active Serpin A10 (SERPINA10)
Gene Names
SERPINA10; PZI; ZPI
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
What Are Active Proteins?
Proteins are large molecules made up of long chains of amino acids.
They will typically fold into a very particular 3-dimensional shape/conformation, that is sometimes referred to as their “native” form, which allows them to work properly in the body. For the purposes of product categorization, AAA Biotech will typically refer to proteins purified from their original animal host as being “native” proteins (this is to signify their difference compared to their “recombinant” or “synthetic” protein counterparts).
If a protein successfully folds into the correct shape, it is will typically display high fidelity characteristics to its original protein in its original animal host, and be classified as an active protein, as it will be able to function “normally” in most enzymatic or binding capacities. If it loses this shape, due to factors such as heat or strong chemicals (such as detergents), it becomes inactive and is no longer able to perform its basic functions. All of the proteins in this category are made under strict quality control, and they are active, pure, low in contaminants, and stable.
Most are stored as freeze-dried powders and come without extra tags, so they’re very close to the actual natural/native form.
Key Applications of Active Proteins
1. Scientific Research
- Aid in the study of how proteins function in the body
- Aid in understanding various disease processes
2. Drug Development
- Powerful tools to investigate how potential drugs interact with specific proteins
- Ideal for identifying drug targets
3. Cell Culture
- Are routinely utilized to support cell growth and function (e.g., using exogenous growth factors)
- Can be used to promote cellular development into specific types (differentiation)
4. Diagnostics
- Regularly utilized in tests to detect diseases or infections (e.g., COVID-19, cancer)
- Note: All products are strictly for research-use only (RUO).
5. Therapeutics
- Some active proteins are used directly as treatments (e.g., insulin, enzymes)
- Note: All products are strictly for research-use only (RUO).
6. Vaccine Development
- Used to create or test vaccines by mimicking parts of viruses or bacteria
7. Biochemical Assays
- They can facilitate the characterization of enzyme activity, binding strength, or protein interactions in lab tests
Why Buy Active Proteins from AAA Biotech?
- High biological activity – Verified to perform as expected or indicated on datasheet
- Strict quality control – We are confident in our active proteins’ reliability and consistency
- High purity & low endotoxin – Ideal for applications involving sensitive or precious samples/components
- Freeze-dried for stability – Long shelf life and straightforward storage
- Mostly tag-free – Closer to natural/native protein form
FAQ
1. What are active proteins used for in research?
Active proteins are used primarily in the study of how proteins function, in characterizing/discovering drug interactions, supporting cell growth, running biochemical assays, and in development of diagnostics or therapeutics.
2. How are AAA Biotech's active proteins validated?
AAA Biotech’s active proteins are validated through strict quality control and functional assays to ensure they are properly folded and active. “Active”, though, can be an ambiguous term, so if a specific “activity” or “binding” capability of a protein is of crucial interest to you, please inquire with us prior to purchase, and we will provide further details on how the “Active” modifier was determined to be applicable.
3. Are these proteins tested for biological activity?
Yes, all active proteins from AAA Biotech are tested to confirm they have the expected biological activity before being offered for use. Though, said “biological activity” can be either “enzymatic”, “binding”, or both.