AAA Biotech 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.
98.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel. (d) Gel filtration chromatography under non denaturing conditions.
SDS-PAGE (Sample: Active recombinant ADIPOR1, Human)
Gene Sequencing (extract)
Activity (ADIPOR1 (Adiponectin receptor protein 1) is a receptor for ADP (30kDa adipocyte complement-related protein), an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Besides, human ADP and rat ADP exist similarities in amino acid sequence with the identity of 83.2%. Thus a binding ELISA assay was conducted to detect the interaction of recombinant human ADIPOR1 and recombinant rat ADP. Briefly, ADIPOR1 were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to ADP-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-ADIPOR1 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 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of ADIPOR1 and ADP was shown in Figure 1, and this effect was in a dose dependent manner.)
SDS-PAGE (Sample: Active recombinant MASP2, Human)
Gene Sequencing (extract)
Activity (MASP2 (Mannan-binding lectin serine protease 2) is a serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. The preproprotein of MASP2 is proteolytically processed to generate A and B chains that heterodimerize to form the mature protease, which is able to associate with MBL2. Thus, a functional binding ELISA assay was constructed to detect the association of rhMASP2 with MBL2. Briefly, rhMASP-2 were diluted serially in 10mM Tris-HCl, 1M NaCl, 5mM CaCl2, and 0.05%Triton X-100 (pH 7.4). Duplicate samples of 100uL were then transferred to MBL2-coated microtiter wells and incubated for 2h at 37oC. Wells were washed with PBST and incubated for 1h with anti-MASP-2 pAb, then aspirated and washed 3 times. After incubation with HRP labeled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution , wells were incubated for 15-25 minutes at 37oC. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of MASP2 with MBL2 was shown in Figure 1 and this effect was in a dose dependent manner.)
WB (Western Blot) (Positive WB detected in: His tag-tagged SARS-CoV-2 nucleocapsid recombinant protein from E. Coli SARS-CoV-2 nucleocapsid antibody at 1:1000; Secondary; Peroxidase-Affinipure Goat Anti-Human IgG, Fc? Fragment Specific at 1/20000 dilution; Predicted band size: 48 kDa; Observed band size: 55 kDa)
Biological Activity (Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-N at 5 ug/ml can bind SARS-CoV-2-N Antibody, the EC50 of SARS-CoV-2-N protein is 43.50-118.4 ng/ml.)
SDS-PAGE ((Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.)
SDS-Page (SDS-PAGESample: Active recombinant GAL9, Human)
Application Data (Gene Sequencing (extract))
Application Data (Inhibition of Jurkat cells proliferation after stimulated with GAL9.)
Application Data (GAL9 also can induce cellular apoptosis. To test the effect of GAL9 on cell apoptosis, Jurkat cells were seeded into 96-well plates at a density of 5,000 cells/well with 2% serum standard RPMI 1640 including various concentrations of recombinant human GAL9. After incubated for 48 h, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 20 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 4 h at 37 degree C. Proliferation of Jurkat cells after incubation with GAL9 for 48 h observed by inverted microscope was shown in Figure 3. Cell viability was assessed by CCK-8 assay after incubation with recombinant human GAL9 for 48 h. The result was shown in Figure 4. It was obvious that GAL9 significantly inhibit cell viability of Jurkat cells. The ED50 is 1.64 ug/mL.Inhibition of Jurkat cells proliferation after stimulated with GAL9(A) Jurkat cells cultured in RPMI 1640, stimulated with 2.5ug/mL GAL9 for 48h;(B) Unstimulated Jurkat cells cultured in RPMI 1640 for 48h.)
Application Data (The hemagglutination assay of GAL9 in V- bottom shaped 96-well microtiter plate)
Activity (Galectin 9 (GAL9) is a member of the Beta-galactoside-binding galectin family. Galectin-9 is found outside of cells and may be exported by non-classical pathways. Galectin 9 exhibits a variety of biological activities, the majority of which have focused on its immunomodulatory role toward lymphocytes, were it shows specific interactions with TIM-3, and can negatively regulate Th1 type immunity. It also can agglutinate red blood. In this case, we chose rabbit erythrocyte (RaE) to assay its ability of agglutination. A general procedure for hemagglutination assay (or haemagglutination assay; HA) is as follows, two-fold dilute the recombinant human GAL9 with 0.01M PBS(pH7.4), add 50ul a serial dilution of GAL9 to each well of a U or V- bottom shaped 96-well microtiter plate. The final well serves as a negative control with no GAL9, replace with 50uL 0.01M PBS. Then add 50uL 1% rabbit erythrocyte to each well and mixed gently. The plate is incubated for 1-2 hours at room temperature. The results are shown in Figure 1. It was obvious that the minimal effective concentration of GAL9 is 1.5ug/mL.Figure 1.The hemagglutination of recombinant human GAL9(A) Rabbit erythrocyte agglutinated by recombinant human GAL9;(B) Rabbit erythrocyte without recombinant human GAL9.)
SDS-PAGE (Sample: Active recombinant TRAIL, Human)
Gene Sequencing (extract)
Activity Data (Protein TRAIL (TNF-Related Apoptosis-Inducing Ligand) is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. TRAIL induces apoptosis in transformed and tumor cells. This protein binds to several members of TNF receptor superfamily including TNFRSF10B/TRAILR2. Thus a binding ELISA assay was conducted to detect the interaction of TRAIL and TNFRSF10B. Briefly, recombinant human TRAIL were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to TNFRSF10B-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-TRAIL 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 50uL stop solution to the wells and read at 450nm immediately. The binding activity of TRAIL and TNFRSF10B was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (LCAT (Phosphatidylcholine-sterol acyltransferase) is an enzyme in the extracellular metabolism of plasma lipoproteins, which converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines. It is reported that APOA1 (Apolipoprotein A-I) acts as a cofactor for the LCAT. Thus, a binding ELISA assay was conducted to detect the association of LCAT with APOA1. Briefly, recombinant rat LCAT were diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to APOA1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-LCAT 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 50uL stop solution to the wells and read at 450nm immediately. The binding activity of LCAT with APOA1 was shown in Figure 1 and this effect was in a dose dependent manner.)
Activity (Perforin 1 (PRF1) is a pore forming cytolytic protein found in the granules of cytotoxic T lymphocytes (CTLs) and NK cells. Upon degranulation, perforin binds to the target cell's plasma membrane, and oligomerises in a Ca2+ dependent manner to form pores on the target cell. The pore formed allows for the passive diffusion of a family of pro-apoptotic proteases, known as the granzymes, into the target cell. Besides, Calreticulin (CRT) has been identified as an interactor of PRF1, thus a binding ELISA assay was conducted to detect the interaction of recombinant human PRF1 and recombinant human CRT. Briefly, PRF1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to CRT-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PRF1 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 50uL stop solution to the wells and read at 450nm immediately. The binding activity of PRF1 and CRT was shown in Figure 1, and this effect was in a dose dependent manner.The activity of recombinant PRF1 was measured by lysis of erythrocytes using a hemolysis assay. A general procedure is as fllows: two-fold dilute the recombinant human PRF1 with 0.9% NaCl, add 50uL a serial dilution of PRF1, 10uL 0.1M CaCl2 to each well, then add 50uL 0.25% rabbit erythrocyte (RaE) to each well and mixed gently. Add 10uL 0.9% NaCl to reaplace CaCl2 in control wells. The plate is incubated for 20 hours at 37 degree C, 5% CO2. The results are shown in Figure 2. It was obvious that the minimal effective concentration of PRF1 is 12.5ug/mL.)
Mouse super leptin antagonist (mutant D23/L39A/D40A/F41A)
Purity
The purity of mouse super-active leptin antagonist is greater than 98.0% as determined by: (a) Gel filtration analysis. (b) Analysis by reducing and non-reducing SDS-PAGE gel.
SDS-PAGE (SDS-PAGE of ~14 kDa Active Human Recombinant Alpha Synuclein Protein Monomer (SPR-321). Lane 1: Molecular Weight Ladder (MW). Lane 2: BSA (5 ug). Lane 3: BSA (2.5 ug). Lane 4: Active Alpha Synuclein Protein Monomer (5 ug) (SPR-321). Lane 5: Active Alpha Synuclein Protein Monomer (2.5 ug) (SPR-321).)
Application Data (Active alpha synuclein aggregate (SPR-322) seeds the formation of new alpha Synuclein aggregates from the pool of active alpha Synuclein monomers (SPR-321). Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha Synuclein aggregates. 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 alpha Synuclein protein aggregation) over time when 10 nM of active alpha Synuclein aggregate (SPR-322) is combined with 100 uM of active alpha Synuclein monomer (SPR-321), as compared to when 100 uM of control alpha Synuclein monomer (SPR-316) is combined with 10 nM of active alpha Synuclein aggregate (SPR-322). Thioflavin T ex = 450 nm, em = 485 nm.)
SDS-PAGE (Sample: Active recombinant SCF, Porcine)
Identification (Gene Sequence (extract))
Activity (The dose-effect curve of SCF 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 6.07 to 13.69ng/mL.)
Activity (Stem cell factor (SCF), also known as mast cell growth factor (MGF), and steel factor (SLF), plays an important role in hematopoiesis, spermatogenesis, and melanogenesis. SCF 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 1x104cells/well and incubated for 72h in the presence or absence of various concentrations of SCF 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, 10uL of CCK-8 solution was added to each well of the plate, then measure the absorbance at 450nm 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 SCF for 72h observed by inverted microscope was shown in Figure 1.)
Hemagglutination assay (Figure 3. The hemagglutination assay of GAL3 in V- bottom shaped 96-well microtiter plate.)
Effective concentration of GAL3 (Figure 2.GAL3 also can agglutinate red blood. In this case, we chose rabbit erythrocyte (RaE) to assay its ability of agglutination. A general procedure for hemagglutination assay (or haemagglutination assay; HA) is as follows, two-fold dilute the recombinant human GAL3 with 0.01M PBS (pH7.4), add 50uL a serial dilution of GAL3 to each well of a U or V- bottom shaped 96-well microtiter plate. The final well serves as a negative control with no GAL3, replace with 50uL 0.01M PBS. Then add 50uL 1% rabbit erythrocyte to each well and mixed gently. The plate is incubated for 1-2 hours at room temperature. The results are shown in Figure 2. It was obvious that the minimal effective concentration of GAL3 is 1.2ug/mL.)
Activity (Figure 1.Galectin 3 (GAL3) is a member of the lectin family, of which 14 mammalian galectins have been identified. It is also a member of the beta-galactoside-binding protein family that plays an important role in cell-cell adhesion, cell-matrix interactions, macrophage activation, angiogenesis, metastasis, apoptosis. The protein also has been demonstrated to be involved in cancer, inflammation and fibrosis, heart disease, and stroke. GAL3 is expressed in the nucleus, cytoplasm, mitochondrion, cell surface, and extracellular space. Besides, Alpha-2-Heremans Schmid Glycoprotein (aHSG) has been identified as an interactor of GAL3, thus a binding ELISA assay was conducted to detect the interaction of recombinant human GAL3 and recombinant human aHSG. Briefly, GAL3 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to aHSG-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GAL3 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 50uL stop solution to the wells and read at 450nm immediately. The binding activity of GAL3 and aHSG was shown in Figure 1, and this effect was in a dose dependent manner.)
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.
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