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.
Bioactivity (HTRF assay for MAP2K1 (MEK1) activity 1 uM TK substrate was incubated with different concentrations of MAP2K1 (MEK1) protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. Then 10 ul detection reagents containing anti-TK antibody and SAXL665 (each of which was 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 KinEASE TK assay was used to detect the enzymatic activity.)
SDS-PAGE (Recombinant MAP2K1 (MEK1 protein 10% SDS-PAGE with Coomassie blue staining MW: 46.8 kDa Purity: >80%)
Bioactivity (HTRF assay for RPS6KA2/RSK3 protein activity 1 uM STK S1 substrate was incubated with different concentrations of RPS6KA2/RSK3 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 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 RPS6KA2/RSK3 protein activity 1 uM STK S1 substrate was incubated with different concentrations of RPS6KA2/RSK3 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 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 PRKD2 activity. 1 uM STK S1 substrate was incubated with different concentrations of PRKD2 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 PRKD2 activity. 1 uM STK S1 substrate was incubated with different concentrations of PRKD2 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 PRKD2 protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 98 kDa Purity: >80%)
Bioactivity (HTRF Assay for Recombinant PLK1 activity. 1 uM STK S1 substrate was incubated with different concentrations of PLK1 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 PLK1 activity. 1 uM STK S1 substrate was incubated with different concentrations of PLK1 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 PLK1 protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 69.5 kDa Purity: >80%)
Application Data (KRAS G12V (HLA-A*03:01) Tetramer SPRSPR image shows curve for KRAS G12V(HLA-A*03:01) and immobilized Antibody binding, with a calculated affinity constant of 42nM)
Application Data (KRAS G12V (HLA-A*03:01) Tetramer HPLCThe purity of KRAS G12V (HLA-A*03:01)complex tetramer was greater than 95% as determined by SEC-HPLC.)
SDS-PAGE (KRAS G12V (HLA-A*03:01)Tetramer protein PAGE1ug loaded Tris-Bis PAGE under reducing condition. The purity is greater than 95%.)
Application Data (Polarized membrane extensions mediate osteoclast fusion.(D, top) Immunoblot analysis of lysates of RAW264.7 macrophages stimulated with RANKL for the indicated times with antibodies to Ser473-phosphorylated (p) or total forms of Akt.)
Application Data (Expression of pro-resorptive cytokines in gouty tophus tissues.(c) Immunofluorescent stains for CD3 (green) and RANKL (red) in tophaceous gout tissues.)
Application Data (PLC?2 is required for in vitro osteoclast development.(a) Representative TRAP-stained images of wild-type and PLC?2?/? bone marrow cells cultured in the presence of the indicated concentrations of recombinant murine M-CSF and RANKL for 4 days.)
Application Data (Generation of conditional TAK1-deficient mice.Colony formation by BM cells from Map3k7)
Application Data (G-CSF production by various mouse tumor models.Sera G-CSF levels determined from nontumor-bearing mice (n?=?10), mice treated with recombinant G-CSF protein (10 ug daily for 5 consecutive days) (n?=?8) or mice bearing 4T1 cells (n?=?9) or AT-3 tumor cells pooled from two separate experiments (n?=?9; overall tumor volume ?2cm3).)
Application Data (Inhibition of neutrophil differentiation by IRF4.Wright-Giemsa staining of 32Dcl.3 cells transduced with empty MSCV-puro, MSCV-IRF4DYKDDDDK-puro or MSCV-IRF8DYKDDDDK-puro and cultured in the presence of IL-3 (upper panels) or G-CSF (for 7 days, lower panels).)
Application Data (Expression of programmed death-1 (PD-1) in macrophages/microglia after spinal cord injury (SCI) in mice.Immunohistochemistry in macrophages/microglia 14 days postinjury (dpi) in wild-type mice for (c) PD-1, (d) it’s ligand, PD-L1, and (e) PD-1 in M1 cells [inducible nitric oxide synthase (iNOS)+]; (f) PD-1 in M2 cells [arginase 1 (Arg1+)]; (g) PD-L1 in M1 cells (iNOS+); and (h) PD-L1 in M2 cells (Arg1+).)
Application Data (MPLA-tDCs exhibit a semi-mature surface phenotype and differentially express high levels of TLR-2.TLR-2, PD-L1, GILZ and ILT3 expression on each DC condition was analyzed by flow cytometry to seek for specific tolerogenic DC markers.)
Application Data (In vitro: The proliferative response to recombinant rat VEGF-CC152S was assayed in VEGFR3-expressing porcine aortic endothelial (PAE) cells. Briefly, cells were plated in 12-well plates and incubated in DMEM medium supplemented with 1% fetal calf serum for cell cycle arrest 24h prior to stimulation of cell proliferation with recombinant VEGF-CC152S at the concentrations of 50 and 100 ng/mL. After 48h in culture, the cell proliferative response was assayed (WST-1 colorimetric assay), and the results expressed as % of control non-stimulated cells (mean + sem).)
Application Data (In vivo: The lymphangiogenic response to recombinant rat VEGFCC152S loaded in our biopolymeric albumin-alginate microcapsules for targeted slow-release was assayed in male Wistar rats. Briefly, after ischemiareperfusion injury to induce myocardial infarction, VEGF-CC152S at the dose of 1.5 or 5 ug per heart was injected intra-myocardially. Lymphatic responses in the myocardium were analyzed by IHC at 3 weeks post-MI using LYVE1 antibody. Results are expressed as lymphatic vessel to cardiomyocyte ratio (mean + sem).The experiments were performed by the research group of Prof. Dr. E. Brakenhielm – Rouen University (see also: Henri O et al., Circulation, March 2016, DOI: 10.1161))
SDS-PAGE (SDS-PAGE analysis of recombinant rat VEGF-C152 mutant. Sample was loaded in 15% SDS-polyacrylamide gel under reducing conditions and stained with Coomassie blue.)
Application Data (Binding of recombinant human Wnt5a to recombinant human sROR2 in a functional ELISA. sROR2 was coated with 2ug/ml (100ug/well) and increasing amounts of Wnt5a was added. Detection was performed using a polyclonal rabbit anti-human Wnt5a and a goat anti-rabbit Biotin conjugated secondary antibody.)
SDS-PAGE (SDS-PAGE analysis of recombinant human sROR2 produced in insect cells. Sample was loaded in 15% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.)
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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