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 (1. Measured by its binding ability in a functional ELISA. Immobilized human CD2-His at 10 ug/ml (100 ul/well) can bind human CD58-Fc, The EC50 of human CD58-Fc is 0.04-0.1 ug/ml. 2. Measured by its binding ability in a functional ELISA. Immobilized Cynomolgus CD2-His at 10 ug/ml (100 ul/well) can bind human CD58-Fc, The EC50 of human CD58-Fc is 0.04-0.10 ug/ml.)
Application Data (Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is typically 1-5 ng/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human VEGF121b at 10ug/mL (100uL/well) can bind human VEGFR2-Fc, the EC50 of human VEGFR2-Fc is 0.06-0.1 ug/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human CD47 at 2 ug/ml (100 ul/well) can bind human SIRPa(V2)-His, the EC50 of human SIRPa(V2)-His is 200-800 ng/mL.)
Application Data (Measured by its ability to inhibit BMP9-induced alkaline phosphatase production by MC3T3-E1 cells. The ED50 for this effect is typically 5-15 ng/mL in the presence of 2 ng/mL of recombinant human BMP-9.)
Application Data (Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 10-50 ng/mL in the presence of 10 ng/mL recombinant Activin A.)
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 5-15 ng/mL in the presence of 2 ng/mL of recombiant human BMP9.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized Inhibin Human, Mouse, Rat, Cynomolgus, Rhesus Inhibin beta A/Activin A at 2 ug/ml (100 ul/well) can bind Human ACVR2B hFc, the EC50 of Human ACVR2B hFc is 12-60 ng/mL.)
Activity (As reported, IL-4 will induce the differentiation of THP-1 cells into dendritic cells and macrophages in vitro. THP-1 cells were cultured in RPMI-1640 and stimulated with 2ng/mL IL-4, after 10 days of stimulation, partial cells became larger, grew synapses, and had vesicular bodies intracellular, which showed a morphological characteristics of dendritic cells and macrophages.)
Bioactivity (Netrin 1 (Ntn1) is included in a family of laminin-related secreted proteins. Mouse Ntn1 is a 66-76 kDa glycoprotein that is well known for its involvement in axonal guidance during embryonic development and as an enhancer of cancer cell metastasis. Ntn1 is also involved in outgrowth and migration orientation in the developing CNS and plays a significant role in the morphogenesis of endothelial cells and vascular smooth-muscle cells. It is also involved in the processes of cytoskeleton reorganization, angiogenesis, epithelial cell adhesion, and cell migration in the lungs, mammary gland, and pancreas. Slit Homolog 1 (Slit1) can acts as a potent promoter of both Netrin-1 attractive and repulsive activities on distinct neuronal cell types, thereby opening novel perspectives on the role of combinations of cues in brain wiring. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse Ntn1 and recombinant human Slit1. Briefly, Ntn1 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to Slit1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-Ntn1 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 Ntn1 and recombinant human Slit1 was shown in Figure 1, the EC50 for this effect is 0.03 ug/mL.)
Bioactivity (HTRF assay for Recombinant SETDB1 protein activity. 1 uM histone peptide H3 (1-21) was incubated with SETDB1 in reaction buffer including 50 mM Tris-HCl pH 8.6, 0.02% Triton X-100, 2 mM MgCl2, 1 mM TCEP and 50 uM SAM for 3 hours at room temperature. H3K9me2 antibody was used to detect reaction product.)
Bioactivity (HTRF assay for Recombinant SETDB1 protein activity. 1 uM histone peptide H3 (1-21) was incubated with SETDB1 in reaction buffer including 50 mM Tris-HCl pH 8.6, 0.02% Triton X-100, 2 mM MgCl2, 1 mM TCEP and 50 uM SAM for 3 hours at room temperature. H3K9me2 antibody was used to detect reaction product.)
SDS-PAGE (Recombinant SETDB1 protein gel. SETDB1 protein was run on a 10% SDS-PAGE gel and stained with Coomassie Blue. MW: 145 kDa Purity: > 85%)
Bioactivity (HTRF assay for RPS6KA4/RSK4 activity 1 uM STK S3 substrate was incubated with different concentrations of RPS6KA4/RSK4 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 10 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 RPS6KA4/RSK4 activity 1 uM STK S3 substrate was incubated with different concentrations of RPS6KA4/RSK4 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 10 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 Recombinant NLK activity. 1 uM STK S3 substrate was incubated with different concentrations of NLK protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 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 NLK activity. 1 uM STK S3 substrate was incubated with different concentrations of NLK protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 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 NLK protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 59.5 kDa Purity: >90%)
Bioactivity (HTRF assay for PRKCE; activity 11 uM STK S1 substrate was incubated with different concentrations of PRKCE; protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 10 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 the operations and reactions were performed at room temperature.)
Bioactivity (HTRF assay for PRKCE; activity 11 uM STK S1 substrate was incubated with different concentrations of PRKCE; protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 10 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 the operations and reactions were performed at room temperature.)
Bioactivity (HTRF assay for WNK2 (1-489); activity 1 uM STK S3 substrate was incubated with different concentrations of WNK2 (1-489); protein in a 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 the operations and reactions were performed at room temperature.)
Bioactivity (HTRF assay for WNK2 (1-489); activity 1 uM STK S3 substrate was incubated with different concentrations of WNK2 (1-489); protein in a 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 the operations and reactions were performed at room temperature.)
Bioactivity (HTRF Assay for Recombinant PKN2 activity. 1 uM STK S1 substrate was incubated with different concentrations of PKN2 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 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 PKN2 activity. 1 uM STK S1 substrate was incubated with different concentrations of PKN2 protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 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 PKN2 protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 111.6 kDa Purity: >80%)
Recombinant Human Non-Muscle Myosin-II Regulatory Light Chain
Purity
Greater than 95.0% 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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