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.
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human APOH-his at 2 ug/mL (100 ul/well) can bind biotinylated mouse LDLR-his, The EC50 of biotinylated mouse LDLR-his is 26 ng/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human APOH-his at 2 ug/mL (100 ul/well) can bind biotinylated human LDLR-his, The EC50 of biotinylated human LDLR-his is 0.35 ug/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human TDGF1 at 2 ug/ml (100 ul/well) can bind human ALK-4 with a linear range of 0.032-4 ug/ml.)
Application Data (Measured by its ability to inhibit BMP9 induced alkaline phosphatase production by MC3T3E1 mouse chondrogenic cells. David, L. et al. (2007) Blood 109:1953. The ED50 for this effect is typically 50-200 ng/mL in the presence of 2 ng/mL of recombiant human BMP9.)
Application Data (Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 0.3-2 ug/mL in the presence of 10 ng/mL recombinant Activin A.)
Application Data (Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 0.2-1 ug/mL in the presence of 10 ng/mL recombinant Activin A.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized Mouse Angiopoietin-2-His at 2 ug/ml (100 ul/well) can bind mouse TEK-Fc, the EC50 of mouse TEK-Fc is 350-900 ng/mL.)
Application Data (Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 0.6-3 ug/mL in the presence of 10 ng/ml Recombinant Human Activin A.)
Application Data (Transforming growth factor beta (TGF-) is a multifunctional cytokine belonging to the transforming growth factor superfamily. The TGF- superfamily includes endogenous growth inhibiting proteins; an increase in expression of TGF- often correlates with the malignancy of many cancers and a defect in the cellular growth inhibition response to TGF-. Its immunosuppressive functions then come to dominate, contributing to oncogenesis. To test the effect of TGF- on inhibit HGF-dependent proliferation, HepG2 cells were seeded into triplicate wells of 96-well plates at a density of 2,000 cells/well and allowed to attach, replaced with serum-free overnight, then the medium was replaced with 2% serum standard DMEM including 1ng/mL HGF prior to the addition of various concentrations of recombinant human TGF-. After incubated for 96h, 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 the absorbance at 450nm was measured using a microplate reader after incubating the plate for 1-4 hours at 37. The inhibitory effect of TGF- on HGF-dependent proliferation of HepG2 cells observed by inverted microscope was shown in Figure 2. Cell viability was assessed by CCK-8 assay after incubation with recombinant TGF- for 96h. The result was shown in Figure 3. It was obvious that TGF- significantly decreased cell viability of HepG2 cells. (A) HepG2 cells cultured in DMEM, stimulated with 1ug/mL TGF- for 96h; (B) Unstimulated HepG2 cells cultured in DMEM for 96h.Figure.The inhibitory effect of TGF- on cell proliferation of HepG2 cells.)
ELISA (Biotinylated TGFB-1 ELISAImmobilized Biotinylated Human TGF Beta1 at 1ug/ml (100ul/Well). Response curve for TGFR2 with alinear range of 2-100 ng/ml was determined by ELISA)
Tris-Bis-PAGE (Biotinylated TGFB-1 protein PAGE1ug loaded Tris-Bis PAGE under reducing condition. The purity is greater than 95%.)
ELISA (Functional ELISA to test the binding of sTIE-2 to its ligand Ang-2. Ang-2 was coated on the plate and increasing amounts of recombinant human soluble sTIE-2 was added)
SDS-PAGE (SDS-PAGE analysis of recombinant human soluble TIE-2-Hisproduced from insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue)
Bioactivity (HTRF assay for RPS6KA1/RSK1 activity 1 uM STK S1 substrate was incubated with different concentrations of RPS6KA1/RSK1 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, and 100 uM ATP for 1 hour. The detection reagents were added and incubated with the reactions for 30 min. All operations and reactions were performed at room temperature, and HTRF assay was used to detect the enzymatic activity.)
Bioactivity (HTRF assay for RPS6KA1/RSK1 activity 1 uM STK S1 substrate was incubated with different concentrations of RPS6KA1/RSK1 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, and 100 uM ATP for 1 hour. The detection reagents were added and incubated with the reactions for 30 min. All operations and reactions were performed at room temperature, and HTRF assay was used to detect the enzymatic activity.)
SDS-PAGE (Recombinant RPS6KA1/RSK1 protein gel 10% SDS-PAGE Coomassie staining MW: 84 kDa Purity: >= 90%)
Bioactivity (HTRF Assay for Recombinant PHKG2 activity. 1 uM STK S1 substrate was incubated with different concentrations of PHKG2 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 10 mM MgCl2, 1 mM DTT and 100 uM ATP for 1 hour. The 10 ul detection reagents containing anti-STK antibody (1:2) and SA-XL665 (1:100) diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Bioactivity (HTRF Assay for Recombinant PHKG2 activity. 1 uM STK S1 substrate was incubated with different concentrations of PHKG2 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 10 mM MgCl2, 1 mM DTT and 100 uM ATP for 1 hour. The 10 ul detection reagents containing anti-STK antibody (1:2) and SA-XL665 (1:100) diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
SDS-PAGE (Recombinant PHKG2 protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 47.7 kDa Purity: >70%)
Bioactivity (HTRF Assay for Recombinant BRD2 (BD1+BD2) activity. 3 uM histone peptide H4K5/8/12/16(ac4) was incubated with BRD2 (BD1+BD2) in reaction buffer including 50 mM HEPES-NaOH pH 7.0, 0.1% BSA for 1 hour at room temperature. Anti-His antibody was used to detect reaction products.)
Bioactivity (HTRF Assay for Recombinant BRD2 (BD1+BD2) activity. 3 uM histone peptide H4K5/8/12/16(ac4) was incubated with BRD2 (BD1+BD2) in reaction buffer including 50 mM HEPES-NaOH pH 7.0, 0.1% BSA for 1 hour at room temperature. Anti-His antibody was used to detect reaction products.)
Greater than 98.0% as determined by: (a) Analysis by reducing and non-reducing SDS-PAGE gel. (b) Gel-filtration chromatography under non denaturing conditions.
Rat super leptin antagonist (mutant D23/L39A/D40A/F41A)
Purity
The purity of super rat leptin antagonist is greater than 98.0% as determined by: (a) Gel filtration analysis. (b) Analysis by reducing and non-reducing SDS-PAGE gel.
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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