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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 2300-2350 of 2583 product results
SDS_PAGE
(Sample: Active recombinant GZMK, Mouse)
Granzyme K (GZMK), Active Protein (Cat# AAA161832)
Full Name
Active Granzyme K (GZMK)
Applications
Activity Assay, Cell Culture
Purity
>90%
Pricing
Bioactivity
(Fibrinogen Beta Chain (FGB) is the beta subunit of the coagulation factor fibrinogen, which is a component of the blood clot. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. Fibrinogen Alpha Chain (FGA) has been identified as an interactor of FGB. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human FGB and recombinant mouse FGA. Briefly, FGB was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FGA-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FGB 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 FGB and recombinant mouse FGA was shown in Figure 1, the EC50 for this effect is 0.03 ug/mL.)
Fibrinogen Beta Chain (FGB), Active Protein (Cat# AAA161833)
Full Name
Active Fibrinogen Beta Chain (FGB)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Elastin (ELN) is an extracellular matrix (ECM) protein responsible for the extensibility and elastic recoil of many vertebrate tissues. ELN is abundant in elastic tissues, and tissues rich in elastin include the aorta and major blood vessels, the lungs, elastic ligaments, tendons and the skin. ELN can bind the elastin receptor complex and other receptors and stimulate migration and proliferation of monocytes and skin fibroblasts. Elastokines can also contribute to cancer progression. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS), autosomal dominant cutis laxa. Decorin (DCN), an extracellular matrix (ECM) protein, is one of targets of ECM. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse ELN and recombinant human DCN. Briefly, ELN was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to DCN-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-ELN 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 mouse ELN and recombinant human DCN was shown in Figure 1, the EC50 for this effect is 0.068 ug/mL.)
Elastin (ELN), Active Protein (Cat# AAA161843)
Full Name
Active Elastin (ELN)
Gene Names
Eln; AI385707; AI480567; E030024M20Rik
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), was originally identified as a component of neutrophil granules. It is a 25 kDa protein existing in monomeric and homo- and heterodimeric forms, the latter as a dimer with human neutrophil gelatinases (MMP-9). Its expression has been observed in most tissues normally exposed to microorganism, and its synthesis is induced in epithelial cells during inflammation. Lipocalin-2 has been implicated in a variety of processes including cell differentiation, tumorigenesis, and apoptosis. Studies indicate that Lipocalin-2 binds a bacterial catecholate sidropore bound to ferric ion such as enterobactin with a subnanomolar dissociation constant (Kd = 0.41 nM). The bound ferric enterobactin complex breaks down slowly in a month into dihydroxybenzoyl serine and dihydroxybenzoic acid (DHBA). It also binds to a ferric DHBA complex with much less Kd values (7.9 nM). The activity assay of recombinant human NGAL was measured by its ability to bind Iron(III) dihydroxybenzoic acid Fe(DHBA)3. The binding of Fe(DHBA)3 results in the quenching of Trp fluorescence in Lipocalin-2. The recombinant human NGAL was diluted to 100 ug/ml in assay buffer (50 mM Tris, 10 mM CaCl2, 150 mM NaCl, pH 7.5). 50 uL of the different concentrations of Fe(DHBA)3 and 50 uL of 100 ug/ml rmNGAL was loaded into the plate. Incubated at room temperature for 30 minutes, then read at excitation and emission wavelengths of 280 nM and 340 nM in endpoint mode. The result was shown in Figure 1, the recombinant human Lipocalin-2 can bind >8 uM of Fe(DHBA)3.)
Neutrophil gelatinase-associated lipocalin (NGAL), Active Protein (Cat# AAA161845)
Full Name
Active Neutrophil gelatinase-associated lipocalin (NGAL)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Extracellular matrix metalloproteinase (MMP) inducer (EMMPRIN), also known as basigin and CD147, is a 4466 kDa, variably N and Oglycosylated, type I transmembrane protein that belongs to the immunoglobulin superfamily. EMMPRIN is 269 amino acids (aa) in length and contains a 24 aa signal sequence, a 183 aa extracellular domain (ECD), a 21 aa transmembrane (TM) segment and a 41 aa cytoplasmic tail. The ECD contains one C2type and one Vtype Iglike domain. EMMPRIN is expressed in areas of tissue remodeling, including endometrium, placenta, skin, and regions undergoing angiogenesis. It is also expressed on cells with high metabolic activity, such as lymphoblasts, macrophages and particularly tumor cells. A functional ELISA assay was conducted to detect the interaction of recombinant rat EMMPRIN/CD147 and recombinant human SLC3A2. Briefly, CD147 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to SLC3A2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CD147 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 rat CD147 and recombinant human SLC3A2 was shown in Figure 1, the EC50 for this effect is 0.82 ug/mL.)
Cluster Of Differentiation 147 (CD147), Active Protein (Cat# AAA161852)
Full Name
Active Cluster Of Differentiation 147 (CD147)
Gene Names
Bsg; CE9; HT7; 5A11; Ox47R; EMMPRIN; basignin
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Interleukin-32 (IL-32) is an interleukin cytokine usually linked to inflammation. The IL-32 transcript is expressed in various human tissues and organs such as the spleen, thymus, leukocyte, lung, small intestine, colon, prostate, heart, placenta, liver, muscle, kidney, pancreas, and brain. Cytokines are critical components of cell signaling pathways that are involved in the regulation of cell growth, metabolism, hormone signaling, immune regulation and a variety of other physiological functions. FGFR1 has been identified as an interactor of IL-32, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human IL-32 and recombinant human FGFR1. Briefly, IL-32 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FGFR1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-IL-32 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 IL-32 and recombinant human FGFR1 was shown in Figure 1, the EC50 for this effect is 0.15 ug/mL.)
Interleukin 32 (IL32), Active Protein (Cat# AAA161861)
Full Name
Active Interleukin 32 (IL32)
Gene Names
IL32; NK4; TAIF; TAIFa; TAIFb; TAIFc; TAIFd; IL-32beta; IL-32alpha; IL-32delta; IL-32gamma
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(GSTa2 (Glutathione S-transferase a2) is an enzyme that plays an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. This subfamily of enzymes has a particular role in protecting cells from Reactive Oxygen Species and the products of peroxidation. Polymorphisms in this gene influence the ability of individuals to metabolize different drugs. GSTa3 catalyze the endogenous glutathione conjugation 1-Chloro-2,4-dinitrobenzene (CDNB), which can increase in the absorbance at 340 nm. The reaction was performed in adding 10 ul 200 mM glutathione (reduced) and 10 ul 100 mM CDNB in 980 ul 100 mM NaH2PO4 (pH7.0), rapidly mixed. Then add 50 ul mixed substrates to 50 ul different concentrations of recombinant mouse GSTa2, mix gently. Incubated at 37 degree C for 5min, then read at a wavelength of 340 nm. The specific activity of recombinant mouse GSTa2 is >50000 pmol/min/ug.)
Glutathione S Transferase Alpha 2 (GSTa2), Active Protein (Cat# AAA161869)
Full Name
Active Glutathione S Transferase Alpha 2 (GSTa2)
Gene Names
Gsta2; Gstc2; Gst2-2; Gstc-2
Applications
Activity Assay, Cell Culture
Purity
Greater than 97% by SDS-PAGE
Pricing
Bioactivity
(Telomerase reverse transcriptase (TERT) is a subunit of the enzyme complex telomerase, which adds nucleotides to the ends of telomeres as they become shortened during cell division .Telomerase complex plays a key role in cancer formation by telomere dependent or independent mechanisms. According to statistics, human telomerase reverse transcriptase (h-TERT) is overexpressed in more than 85% of tumors with diverse histologies, with little expression in normal tissues. Expression of h-TERT correlates with activity of telomerase, which is required for the capacity for limitless replication, a hallmark of cancer. The X-Ray Repair Cross Complementing 6 (XRCC6) is high affinity receptor for TERT, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human TERT and recombinant rat XRCC6. Briefly, TERT was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to XRCC6-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-TERT 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 TERT and recombinant rat XRCC6 was shown in Figure 1, the EC50 for this effect is 0.009 ug/mL.)
Telomerase Reverse Transcriptase (TERT), Active Protein (Cat# AAA161880)
Full Name
Active Telomerase Reverse Transcriptase (TERT)
Gene Names
TERT; TP2; TRT; CMM9; EST2; TCS1; hTRT; DKCA2; DKCB4; hEST2; PFBMFT1
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(VCP is an ATPase Associated with diverse cellular Activities (AAA) that has a key role in maintaining cellular homeostasis. VCP is ubiquitously expressed in tissues. At cellular level, VCP functions in many cellular compartments; VCP localizes mainly in the cytoplasm, while a smaller fraction binds to organelles or localizes in the nucleus, where it is implicated in different pathways. VCP assembles and acts as a homo-hexamer, in which each monomer is structured in an N-terminal domain that interacts with adaptors and co-factors; in two ATPase domains, D1 and D2, that by hydrolyzing ATP concur, respectively, in the hexamer formation and in supporting VCP activity; and in a C-terminal domain that binds to a small subset of co-factors and adaptors cooperating with D2 activity. The main role of VCP is to recognize and to extract ubiquitinated proteins from membranes, protein complexes, protein aggregates, or chromatin, modulating their ubiquitination or de-ubiquitination, and to enhance their degradation through the UPS or the autophagic pathway. The activity of recombinant human VCP was measured by its ability to hydrolyze the substrate ATP to phosphate which was detected by the malachite green phosphate detection Kit (Beyotime # S0196M). The reaction was performed in the assay buffer 20 mM HEPES, 13 mM NaCl and 1% glycerol, pH 8.5, initiated by addition 27 uL of various concentrations of VCP (diluted by assay buffer) to 3 uL of 100 mM ATP and 100 mM MgCl2 mixture. The final well serves as a negative control with no VCP, replaced with 27 uL assay buffer. Incubated at 37 degree C for 5min, then stop the reaction by quickly freezing samples in the dry ice and ethanol. 4 ul samples was added to 196 ul assay buffer after thawing at room temperature followed by adding 70 ul phosphate detection agent and incubated at room temperature for 30min, then read at a wavelength of 630 nm. The specific activity of recombinant human VCP is >1000 pmol/min/ug.)
Valosin Containing Protein (VCP), Active Protein (Cat# AAA161891)
Full Name
Active Valosin Containing Protein (VCP)
Gene Names
VCP; p97; TERA; ALS14; IBMPFD
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
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 0.34 ug/mL.)
Luteinizing Hormone (LH), Active Protein (Cat# AAA161735)
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 90% by SDS-PAGE
Pricing
Bioactivity
(Cystatin A (CSTA) is a member of family 1 of the cystatin superfamily. Like Cystatin B, it is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as cathepsins B, H and L. For example, immunohistochemical analysis of Cystatin A and cathepsin L is a useful indicator for malignancy in human epidermal keratinocytes. The ratio of cathepsin B and Cystatin A can be used in the differential identification and treatment of patients with prostate carcinoma. The activity of recombinant mouse Cystatin A 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 mouse Cystatin A (MW: 40.9 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 mouse Cystatin A significantly decreased papain activity. The inhibition IC50 was )
Cystatin A (CSTA), Active Protein (Cat# AAA161736)
Full Name
Active Cystatin A (CSTA)
Gene Names
Csta1; Csta
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Cystatin A (CSTA) is a member of family 1 of the cystatin superfamily. Like Cystatin B, it is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as cathepsins B, H and L. For example, immunohistochemical analysis of Cystatin A and cathepsin L is a useful indicator for malignancy in human epidermal keratinocytes. The ratio of cathepsin B and Cystatin A can be used in the differential identification and treatment of patients with prostate carcinoma. The activity of recombinant pig Cystatin A 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 pig Cystatin A (MW: 40.9 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 pig Cystatin A significantly decreased papain activity. The inhibition IC50 was )
Cystatin A (CSTA), Active Protein (Cat# AAA161737)
Full Name
Active Cystatin A (CSTA)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% 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 human 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 rhTIMP1 (MW: 22.2 KD) was diluted to different concentrations with the assay buffer. Mix 8 ul of rhTIMP1 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 human TIMP1 significantly decreased rhMMP2 activity. The inhibition IC50 was )
Tissue Inhibitors Of Metalloproteinase 1 (TIMP1), Active Protein (Cat# AAA161743)
Full Name
Active Tissue Inhibitors Of Metalloproteinase 1 (TIMP1)
Gene Names
TIMP1; EPA; EPO; HCI; CLGI; TIMP
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% 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 sheep 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 roTIMP1 (MW: 23.2 KD) was diluted to different concentrations with the assay buffer. Mix 8 ul of roTIMP1 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 sheep TIMP1 significantly decreased rhMMP2 activity. The inhibition IC50 was )
Tissue Inhibitors Of Metalloproteinase 1 (TIMP1), Active Protein (Cat# AAA161744)
Full Name
Active Tissue Inhibitors Of Metalloproteinase 1 (TIMP1)
Gene Names
TIMP1; TIMP-1
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Myeloperoxidase (MPO), a member of the XPO subfamily of peroxidases, is a 150 kDa heme protein produced mostly from polymorphonuclear neutrophils and monocytes. MPO is a part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity. Cathepsin S (CTSS) is one of targets of MPO, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human MPO and recombinant bovine CTSS. Briefly, biotin-linked MPO were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CTSS-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 MPO and recombinant bovine CTSS was shown in Figure 1, the EC50 for this effect is 0.16 ug/mL.)
Myeloperoxidase (MPO), Active Protein (Cat# AAA161752)
Full Name
Active Myeloperoxidase (MPO)
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(The cluster of differentiation (CD) antigen CD28 is a member of the immunoglobulin subfamily. CD28 is a central co-stimulatory molecule for TCR-mediated activation such as cytokine production and T-cell proliferation upon ligand binding and TCR stimulation. CD80 and CD86 are expressed on antigen presenting cells and CD86 is primary ligand for CD28. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat CD28 and recombinant human CD86. Briefly, CD28 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CD86-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CD28 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 CD28 and recombinant human CD86 was shown in Figure 1, the EC50 for this effect is 0.07 ug/mL.)
Cluster Of Differentiation 28 (CD28), Active Protein (Cat# AAA161758)
Full Name
Active Cluster Of Differentiation 28 (CD28)
Gene Names
Cd28; CD28RNA
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Homing Associated Cell Adhesion Molecule (HCAM), also known as CD44, is a ubiquitously expressed transmembrane glycoprotein mediating cell responses to the extracellular microenvironment. CD44 is the major surface hyaluronan (HA) receptor, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human CD44 and biotinylated hyaluronan (HA). Briefly, biotin-linked HA were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CD44-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 human CD44 and biotinylated HA was shown in Figure 1, the EC50 for this effect is 0.08 ug/mL.)
Homing Associated Cell Adhesion Molecule (HCAM), Active Protein (Cat# AAA161763)
Full Name
Active Homing Associated Cell Adhesion Molecule (HCAM)
Gene Names
CD44; IN; LHR; MC56; MDU2; MDU3; MIC4; Pgp1; CDW44; CSPG8; HCELL; HUTCH-I; ECMR-III
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% 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 rat HCAM and biotinylated hyaluronan (HA). Briefly, biotin-linked HA were 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 rat 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# AAA161766)
Full Name
Active Homing Associated Cell Adhesion Molecule (HCAM)
Gene Names
Cd44; CD44A; METAA; RHAMM
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Neuropilin 1 (NRP1), as kown as CD304 or VEGF165R, is a 130 - 140 kDa type I transmembrane (TM) glycoprotein. NRP1 is expressed by neurons, blood vessels, immune cells and many other cell types in the mammalian body and binds a range of structurally and functionally diverse extracellular ligands to modulate organ development and function. VEGF165, an angiogenic cytokine, has higher affinity for NRP1. A functional binding ELISA assay was conducted to detect the interaction of recombinant human NRP1 and recombinant human VEGF165. Briefly, NRP1 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to VEGF165-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-NRP1 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 NRP1 and recombinant human VEGF165 was shown in Figure 1, the EC50 for this effect is 2.98 ug/mL.)
Neuropilin 1 (NRP1), Active Protein (Cat# AAA161770)
Full Name
Active Neuropilin 1 (NRP1)
Gene Names
NRP1; NP1; NRP; BDCA4; CD304; VEGF165R
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(The epidermal growth factor receptor (EGFR) is a growth factor receptor that induces cell differentiation and proliferation upon activation through the binding of one of its ligands. The receptor is located at the cell surface, where the binding of a ligand activates a tyrosine kinase in the intracellular region of the receptor. This tyrosine kinase phosphorylates a number of intracellular substrates that activates pathways leading to cell growth, DNA synthesis and the expression of oncogenes such as fos and jun. Epidermal growth factor (EGF) family peptides are ligands for the EGF receptor (EGFR), thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human EGFR and recombinant human EGF. Briefly, biotin-linked EGFR were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to EGF-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 EGFR and recombinant human EGF was shown in Figure 1, the EC50 for this effect is 11.46 ug/mL.)
Epidermal Growth Factor Receptor (EGFR), Active Protein (Cat# AAA161774)
Full Name
Active Epidermal Growth Factor Receptor (EGFR)
Gene Names
EGFR; ERBB; HER1; mENA; ERBB1; PIG61
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 zebrafish 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 zebrafish CRP and recombinant rat F2 was shown in Figure 1, the EC50 for this effect is 0.64 ug/mL.)
C ReProtein (CRP), Active Protein (Cat# AAA161780)
Full Name
Active C Reactive Protein (CRP)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Coagulation Factor IX, also known as Christmas Factor, is a secreted by the liver and plays a key role in the activation of the intrinsic clotting cascade. Factor IX consists of a Gla domain, two tandem EGF-like domains, an activation peptide, and an S1 serine protease domain. Mature human Factor IX shares approximately 81% amino acid sequence identity with mouse and rat Factor IX. Alternative splicing generates an additional isoform that lacks the first EGF-like domain. The activity of recombinant rabbit Coagulation Factor IX is measured by its ability to cleave a fluorogenic peptide substrate Mca-RPKPVE-Nval-WRK(Dnp)-NH2 in the assay buffer 100 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.05% (w/v) Brij-35, pH 8.0. The Coagulation Factor IX is diluted to 100 ug/ml in assay buffer, then activated with a final concentration of 10 ug/ml Thermolysin at 37 degree C for 90min. Adding a final concentration of 10 mM 1,10 Phenanthroline to stop the activation. The activated Coagulation Factor IX is diluted to 6 ug/mL in assay buffer. Loading into a black well plate 50 uL of 6 ug/mL Coagulation Factor IX 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 Coagulation Factor IX. Then read at 320/405 nm in kinetic mode for 5 minutes. The specific activity of recombinant rabbit Coagulation Factor IX is > 20 pmol/min/ug.)
Coagulation Factor IX (F9), Active Protein (Cat# AAA161786)
Full Name
Active Coagulation Factor IX (F9)
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Complement Component 3 (C3) is a vital component of the complement system that plays a central role in immune response and inflammation. C3 is a b2 globulin synthesized by the liver, whose structure consists of two polypeptide chains, a and b, and is the most abundant complement component in serum. It has reported that P-Selectin (SELP) can interact with C3, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse C3 and recombinant human SELP. Briefly, biotin-linked SELP were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to C3-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. When Recombinant mouse C3 is lmmobilized at 2 ug/mL (100 uL/well), the concentration of human SELP that produces 50% optimal binding response is found to be approximately 3.75 ug/mL.)
Complement Component 3 (C3), Active Protein (Cat# AAA161794)
Full Name
Active Complement Component 3 (C3)
Gene Names
C3; ASP; Plp; HSE-MSF; AI255234
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Complement Component 1, Q Subcomponent A (C1qA) is a protein that plays a crucial role in the innate immune system. It is part of the C1 complex, which is the first component of the classical complement pathway. The C1 complex is composed of one molecule each of C1q, C1r, and C1s. C1q is the recognition subcomponent of the complex and and initiating the complement cascade. C1qA plays a key role in eliminating pathogens, regulating inflammatory response and maintaining immune tolerance. It is reported that C1qA can bind to the C-terminal of CALR through its gelatin-as-region, and this interaction may play an important role in regulating complement activation and cell signaling. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse C1qA and recombinant human CALR. Briefly, C1qA was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CALR-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-C1qA 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 mouse C1qA and recombinant human CALR was shown in Figure 1, the EC50 for this effect is 0.03 ug/mL.)
Complement Component 1, Q Subcomponent A (C1qA), Active Protein (Cat# AAA161911)
Full Name
Active Complement Component 1, Q Subcomponent A (C1qA)
Gene Names
C1qa; C1q; AI255395
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(N-Acetyltransferase 2 (NAT2)) is an enzyme that plays an important role in metabolism and detoxification of many compounds including drugs and environmental carcinogens through chemical modification of the amine group with an acetyl group. Cytochrome P4502E1 (CYP2E1) and NAT2 are related to chronic obstructive pulmonary disease and CYP2E1 can bind to NAT2. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat NAT2 and recombinant mouse CYP2E1. Briefly, NAT2 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CYP2E1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-NAT2 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 NAT2 and recombinant mouse CYP2E1 was shown in Figure 1, the EC50 for this effect is 0.096 ug/mL.)
N-Acetyltransferase 2 (NAT2), Active Protein (Cat# AAA161924)
Full Name
Active N-Acetyltransferase 2 (NAT2)
Gene Names
Nat2; Nat2a
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Tissue inhibitors of metalloproteinases or TIMPs are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four members of the family, TIMP-1, TIMP-2, TIMP-3, and TIMP-4. TIMP-2 is a non N-glycosylated protein with a molecular mass of 22 kDa produced by a wide range of cell types, which inhibits MMPs non-covalently by the formation of binary complexes. TIMP-2 also has erythroidpotentiating and cell growth promoting activities. The activity of recombinant chicken TIMP2 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 rgTIMP2 (MW: 23 KD) was diluted to different concentrations with the assay buffer. Mix 8 ul of rgTIMP2 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 chicken TIMP2 significantly decreased rhMMP2 activity. The inhibition IC50 was )
Tissue Inhibitors Of Metalloproteinase 2 (TIMP2), Active Protein (Cat# AAA161696)
Full Name
Active Tissue Inhibitors Of Metalloproteinase 2 (TIMP2)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Figure 2. The dose-effect curve of rmTPO on MO7e cells)
Thrombopoietin (TPO), Active Protein (Cat# AAA161704)
Full Name
Active Thrombopoietin (TPO)
Gene Names
Thpo; Ml; Tpo; Mgdf; Tpo1; Tpo2; Tpo3; Tpo4; Mpllg
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Urokinase Plasminogen Activator (uPA), also known as u-plasminogen activator or urokinase, is a highly-specific serine protease from the peptidase S1 family that cleaves plasminogen to form plasmin making it a key player in the plasminogen activator (PA) system. Expression of uPA is minimal in normal cells but is increased several fold in tumor cells by extracellular stimuli elevated in cancer and corresponds to poor outcomes in several types of cancer. Therefore, uPA has been identified as an excellent target for therapeutic development through inhibition of protease activity or though inhibition of uPA-dependent signaling while in complex with uPA receptor (uPAR). The activity assay of uPA was measured by its ability to cleave a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC). The reaction was performed in 50 mM Tris, 0.01% Tween-20, pH 8.5 (Assay Buffer), ainitiated by addition 50 uL of 1.5 ug/ml uPA (diluted by Assay Buffer) to 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 uPA is >700 pmol/min/ug.)
Plasminogen Activator, Urokinase (uPA), Active Protein (Cat# AAA161707)
Full Name
Active Plasminogen Activator, Urokinase (uPA)
Gene Names
Plau; uPA; u-PA
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Neutrophil elastase (NE), also known as polymorphonuclear leukocyte elastase, is a major protease in the primary granules of neutrophils, is involved in microbicidal activity. It is located primarily in the azurophil granules of polymorphonuclear leukocytes. NE is an important factor promoting inflammation, has bactericidal effects, and shortens the inflammatory process. NE also regulates tumor growth by promoting metastasis and tumor microenvironment remodeling. However, NE plays a role in killing tumors under certain conditions and promotes other diseases such as pulmonary ventilation dysfunction. Additionally, it plays a complex role in various physiological processes and mediates several diseases. Lactoferrin (LTF) has been identified as an interactor of NE, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat NE and recombinant goat LTF. Briefly, biotin-linked NE were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to LTF-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 rat NE and recombinant goat LTF was shown in Figure 1, the EC50 for this effect is 1.19 ug/mL.)
Neutrophil Elastase (NE), Active Protein (Cat# AAA161713)
Full Name
Active Neutrophil Elastase (NE)
Gene Names
Elane; Ela2
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(GLB1 is a lysosomal beta -galactosidase that hydrolyzes the terminal beta -galactose from ganglioside and keratan sulfate. Defects in this gene are the causes of lysosomal storage diseases for GM1-gangliosidosis and Morquio B syndrome (also known as mucopolysaccharidosis IVB). In GM1 gangliosidosis, GM1 ganglioside accumulates in the neurons of the central nervous system, because of the deficiency of lysosomal beta -galactosidase activity. GM1 gangliosidosis demonstrates varying degrees of clinical severity but is invariably fatal, and children with the most common and severe form of GM1 gangliosidosis usually die within 3 years of birth. Morquio B syndrome patients are neurologically normal, but display severe skeletal dysostosis multiplex because of an accumulation of keratan sulfate. The activity assay of GLB1 was measured by its ability to cleave a peptide substrate, 4-Methylumbelliferyl-beta -D-galactopyranoside. The reaction was performed in 50 mM Sodium Citrate, pH 3.5 (Assay Buffer), ainitiated by addition 50 uL of 1.5 ug/ml uPA (diluted by Assay Buffer) to 50 uL of 1.2 mM Substrate. Read at excitation and emission wavelengths of 365 nm and 445 nm (top read), respectively, in kinetic mode for 5 minutes. The specific activity of recombinant mouse GLB1 is >17000 pmol/min/ug.)
Galactosidase Beta (GLb), Active Protein (Cat# AAA161714)
Full Name
Active Galactosidase Beta (GLb)
Gene Names
Glb1; Bge; Bgl; Bgs; Bgt; Bgl-e; Bgl-s; Bgl-t; AW125515; C130097A14Rik
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Gelsolin (GSN), one of the most abundant actin-binding proteins, is a multifunctional regulator of physiological and pathological cellular process and regulate cell migration, cell morphology, proliferation and apoptosis. Widely expressed, Gelsolin binds to actin and fibronectin, and is found both secreted in plasma and in cytoplasm and a previous study revealed that the levels of GSN are decreased in various cancer. Profilin-1 (PFN1) can also bind to actin and affects the structure of the cytoskeleton. PFN1 is one of the ligands of GSN, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human GSN and recombinant human PFN1. Briefly, GSN was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PFN1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GSN 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 GSN and recombinant human PFN1 was shown in Figure 1, the EC50 for this effect is 1.11 ug/mL.)
Gelsolin (GSN), Active Protein (Cat# AAA161725)
Full Name
Active Gelsolin (GSN)
Gene Names
GSN; ADF; AGEL
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Complement Component 4a (C4a) is a component of the complement system, which is a cleavage product of the complement C4 protein. C4a has been implicated in various inflammatory and immune responses. It acts as a chemoattractant, recruiting immune cells such as neutrophils and macrophages to the site of inflammation. Additionally, C4a can stimulate the release of pro-inflammatory cytokines and chemokines, further amplifying the immune response. C4a and C4b are the two subunits of C4, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human C4a and recombinant mouse C4b. Briefly, C4a was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to C4b-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-C4a 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 C4a and recombinant mouse C4b was shown in Figure 1,and this effect was in a dose dependent manner.)
Complement Component 4a (C4a), Active Protein (Cat# AAA161728)
Full Name
Active Complement Component 4a (C4a)
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
(Figure 2. Inhibition of HepG2 cells proliferation after stimulated with recombinant bovine BMP4)
Bone Morphogenetic Protein 4 (BMP4), Active Protein (Cat# AAA161652)
Full Name
Active Bone Morphogenetic Protein 4 (BMP4)
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 human BMP4)
Bone Morphogenetic Protein 4 (BMP4), Active Protein (Cat# AAA161654)
Full Name
Active Bone Morphogenetic Protein 4 (BMP4)
Gene Names
BMP4; ZYME; BMP2B; OFC11; BMP2B1; MCOPS6
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Endothelial protein C receptor (EPCR) also known as CD201, is a transmembrane glycoprotein expressed on vascular endothelial cells and functions as a negative regulator of thrombosis. It is expressed most strongly in the endothelial cells of arteries and veins in heart and lung. Mature human EPCR consists of a 193 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 7 aa cytoplasmic tail. Within the ECD, human EPCR shares 63% and 66% aa sequence identity with mouse and rat EPCR, respectively. EPCR inhibits thrombosis through its interactions with Protein C, activated Protein C (APC), and Coagulation Factors VII, and VIIa. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human EPCR and recombinant rat Coagulation Factor VII (F7). Briefly, EPCR was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to F7-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-EPCR 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 EPCR and recombinant rat F7 was shown in Figure 1, the EC50 for this effect is 0.06 ug/mL.)
Endothelial protein C receptor (EPCR), Active Protein (Cat# AAA161658)
Full Name
Active Endothelial protein C receptor (EPCR)
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Figure 3. Cell proliferation of MCF-7 cells after stimulated with IGF1.)
Insulin Like Growth Factor 1 (IGF1), Active Protein (Cat# AAA161670)
Full Name
Active Insulin Like Growth Factor 1 (IGF1)
Gene Names
Igf1; Igf-1; Igf-I; C730016P09Rik
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Insulin-like growth factor 2 (IGF2) is one of three protein hormones that share structural similarity to insulin. It has growth-regulating, insulin-like and mitogenic activities.IGF2 exerts its effects by binding to the IGF-1 receptor and to the short isoform of the insulin receptor. IGF2 may also bind to the IGF2 receptor (also called the cation-independent mannose 6-phosphate receptor), which acts as a signalling antagonist; that is, to prevent IGF2 responses. Besides, Insulin Receptor (INSR) has been identified as an interactor of IGF2, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat IGF2 and recombinant human INSR. Briefly, IGF2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to INSR-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-IGF2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, 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 50uL stop solution to the wells and read at 450 nm immediately. The binding activity of recombinant rat IGF2 and recombinant human INSR was shown in Figure 1, the EC50 for this effect is 0.71 ug/mL.)
Insulin Like Growth Factor 2 (IGF2), Active Protein (Cat# AAA161672)
Full Name
Active Insulin Like Growth Factor 2 (IGF2)
Gene Names
Igf2; IGFII; RNIGF2
Applications
Activity Assay, Cell Culture
Purity
Greater than 97% by SDS-PAGE
Pricing
Bioactivity
(Leptin is a hormone made by adipose cells that helps to regulate energy balance by inhibiting hunger. Many of leptin's effects are mediated through neuropeptide-containing neurons and neuropeptide receptors in the hypothalamus. Although regulation of fat stores is deemed to be the primary function of leptin, it also plays a role in other physiological processes, as evidenced by its multiple sites of synthesis other than fat cells, and the multiple cell types beside hypothalamic cells that have leptin receptors. A functional binding ELISA assay was conducted to detect the interaction of recombinant mouse LEP and recombinant human LEPR. Briefly, LEP were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to LEPR-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-LEP pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 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 of LEP and LEPR was shown in Figure 1, the EC50 for this effect is 0.26 ug/mL.)
Leptin (LEP), Active Protein (Cat# AAA161681)
Full Name
Active Leptin (LEP)
Gene Names
Lep; ob; obese
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Oncostatin M (OSM) is an approximately 30 KDa secreted cytokine belonging to the Interleukin-6 family. Like other members of the IL-6 family such as IL-11, CNTF, and Cardiotrophin-1, OSM plays crucial roles in inflammation, neuroprotection, hematopoiesis, metabolism and development. To test the effect of OSM on cell proliferation, TF-1 cells were seeded into triplicate wells of 96-well plates with various concentrations of recombinant human OSM. After incubated for 72 hours, 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 1-4 hours at 37 degree C. Proliferation of TF-1 cells after incubation with OSM for 72 hours 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 human OSM for 72 hours. The result was shown in Figure 2. It was obvious that recombinant human OSM significantly increased cell viability of TF-1 cells, the EC50 was 0.014 ug/ml.)
Oncostatin M (OSM), Active Protein (Cat# AAA161689)
Full Name
Active Oncostatin M (OSM)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
TGF beta 1, Active Protein (Cat# AAA174043)
Full Name
Recombinant Rat TGF beta 1 Protein
Gene Names
Tgfb1; Tgfb
Purity
>90% as determined by SDS-PAGE
Pricing
SDS-PAGE
Neurexin-3-beta / NRXN3, Active Protein (Cat# AAA173540)
Full Name
Recombinant Human NRXN3 Protein (His Tag)(Active)
Gene Names
NRXN3; C14orf60
Purity
> 94 % as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
LIMP-2 / SCARB2 / CD36L2, Active Protein (Cat# AAA173552)
Full Name
Recombinant Human LIMP-2 / SCARB2 / CD36L2 Protein (His & Fc tag)
Gene Names
SCARB2; AMRF; EPM4; LGP85; CD36L2; HLGP85; LIMP-2; LIMPII; SR-BII
Purity
> 90 % as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
ICOS / AILIM / CD278, Active Protein (Cat# AAA173569)
Full Name
Recombinant Human ICOS / AILIM / CD278 Protein (His & Fc tag)
Gene Names
ICOS; AILIM; CD278; CVID1
Purity
>90% as determined by SDS-PAGE
Pricing
SDS-PAGE
IL-1 beta / IL1B, Active Protein (Cat# AAA173575)
Full Name
Recombinant Human IL-1 beta / IL1B Protein (pro form, His tag)
Gene Names
IL1B; IL-1; IL1F2; IL1-BETA
Purity
>95 % as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
VEGFR2 / Flk-1 / CD309 / KDR, Active Protein (Cat# AAA173577)
Full Name
Recombinant Human VEGFR2 / Flk-1 / CD309 / KDR Protein (His tag)
Gene Names
KDR; FLK1; CD309; VEGFR; VEGFR2
Purity
> 97 % as determined by SDS-PAGE
Pricing
Butyrylcholine Esterase, Active Protein (Cat# AAA174587)
Full Name
Recombinant Human Butyrylcholine Esterase Protein
Gene Names
BCHE; E1; CHE1; CHE2; BCHED
Purity
>95% as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
CTLA4/CD152, Active Protein (Cat# AAA174705)
Full Name
Recombinant Human CTLA4 Protein (His Tag)(Active)
Gene Names
CTLA4; CD; GSE; GRD4; ALPS5; CD152; CTLA-4; IDDM12; CELIAC3
Purity
> 95% as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
NAD-dependent malic enzyme, mitochondrial protein (ME2), Active Protein (Cat# AAA114230)
Full Name
Recombinant Human NAD-dependent malic enzyme, mitochondrial protein (ME2) (Active)
Gene Names
ME2; ODS1
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
SDS-PAGE
C-X-C motif chemokine 6 protein (CXCL6), Active Protein (Cat# AAA114233)
Full Name
Recombinant Human C-X-C motif chemokine 6 protein (CXCL6) (Active)
Gene Names
CXCL6; GCP2; CKA-3; GCP-2; SCYB6
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
SDS-PAGE
Interleukin-8 (CXCL8), Active Protein (Cat# AAA114238)
Full Name
Recombinant Human Interleukin-8 (CXCL8), partial (Active)
Gene Names
CXCL8; IL8; NAF; GCP1; LECT; LUCT; NAP1; GCP-1; LYNAP; MDNCF; MONAP; NAP-1
Purity
Greater or equal to 85% purity as determined 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.