At AAA Biotech, we offer a comprehensive selection of high-quality recombinant proteins for use in a wide range of research areas, including immunology, neuroscience, stem cell research, cancer research and more. No matter whether you need recombinant proteins for cell expansion, polarization, differentiation, or cell processing applications, we have got you covered.
Our recombinant proteins undergo rigorous quality testing. So, you can rely on AAA Biotech for high-quality recombinant proteins to support your research. Explore our catalog to find the right protein for your research needs.
ELISA (Biotinylated Human NKG2A/CD159a Protein ELISA DataImmobilized Anti-NKG2A Antibody, hFc Tag at 2?g/ml (100?l/well) on the plate. Dose response curve for Biotinylated Human NKG2A, His Tag with the EC50 of 0.21?g/ml determined by ELISA.)
Tris-Bis-PAGE (Biotinylated Human NKG2A/CD159a Protein Tris-Bis PAGEBiotinylated Human NKG2A on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.)
ELISA (Biotinylated Human NKG2A&CD94 Protein ELISA DataImmobilized Anti-NKG2A Antibody, hFc Tag at 1?g/ml (100?l/Well) on the plate. Dose response curve for Biotinylated Human NKG2A&CD94, His Tag with the EC50 of 0.11?g/ml determined by ELISA.)
Application Data (Biotinylated Human NKG2A&CD94 Protein SEC-HPLCThe purity of Biotinylated Human NKG2A&CD94 is greater than 95% as determined by SEC-HPLC.)
Tris-Bis-PAGE (Biotinylated Human NKG2A&CD94 Protein Tris-Bis PAGEBiotinylated Human NKG2A&CD94 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.)
ELISA (Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein ELISA DataImmobilized Anti-TRAIL R2 Antibody, hFc Tag at 5?g/ml (100?l/well) on the plate. Dose response curve for Biotinylated Human TRAIL R2, His Tag with the EC50 of 0.1?g/ml determined by ELISA.)
Application Data (Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein SEC-HPLCThe purity of Biotinylated Human TRAIL R2 is greater than 95% as determined by SEC-HPLC.)
Tris-Bis-PAGE (Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein Tris-Bis PAGEBiotinylated Human TRAIL R2 on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.)
ELISA (Biotinylated Human FGFR2 beta (IIIb) Protein ELISA DataImmobilized Anti-FGFR2 IIIb Antibody, hFc Tag at 1?g/ml (100?l/well) on the plate. Dose response curve for Biotinylated Human FGFR2 beta (IIIb) , His Tag with the EC50 of 13.1ng/ml determined by ELISA.)
Application Data (Biotinylated Human FGFR2 beta (IIIb) Protein SEC-HPLCThe purity of Biotinylated Human FGFR2 beta (IIIb) is greater than 95% as determined by SEC-HPLC.)
Tris-Bis-PAGE (Biotinylated Human FGFR2 beta (IIIb) Protein Tris-Bis PAGEBiotinylated Human FGFR2 beta (IIIb) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.)
SDS-PAGE (Figure 2 : SDS-PAGE analysis of purified Human ACE2 His and DYKDDDDK Tag recombinant protein. 4 ug protein was run on a 4-20% SDS-PAGE gel followed by Coomassie blue staining.)
Application Data (Figure 1 : Recombinant Human ACE2 His and DYKDDDDK Tag (21-1006) binds with high affinity to the Spike (RBD) protein of the virus SARS-CoV-2. Method: Recombinant Human ACE2 His and DYKDDDDK Tag (21-1006) is coated on an ELISA plate at 1ug/ml overnight at 4 degree C. Recombinant SARS-Cov-2 Spike RBD Protein Fc Tag (319-541 aa) is added (starting at a concentration of 500 ng/ml with a two fold serial dilution) incubated one hour at RT. The interaction is then detected using an anti-human IgG (HRP).)
Application Data (Figure-3:Comparative binding of Spike S1 variants to sACE2: Wells of a 96-well microtiter plate were coated with 100 ng in duplicates each of S1-WT, S1-N439K, S1-D614G, S1-South Africa, and S1-Southern California. Binding to sACE2 was determined by adding different concentrations of biotinylated-sACE2.)
WB (Western Blot) (Figure-2: Western blot analysis of recombinant SARS-CoV-2 Spike S1 N439K mutant protein. Anti-Spike S1 antibody was used in western Blot analysis.)
Application Data (Figure-1: Recombinant SARS-CoV-2 Spike S1 N439K mutant protein was run on a 4-20% SDS-PAGE gel followed by Coomassie blue staining.)
Application Data (HTRF assay for p53 (TP53) activity 1 uM oligo ds DNA (sequence: 5’-CCGGACATGCCCGGGCATGT-3’) was incubated with BSA for 1 hour, then 10 ul DYKDDDDK antibody and SA-XL665 mixture (each 1:100 dilution in binding buffer) was added to each reaction system and incubated for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Application Data (HTRF assay for p53 (TP53) activity 1 uM oligo ds DNA (sequence: 5’-CCGGACATGCCCGGGCATGT-3’) was incubated with BSA for 1 hour, then 10 ul DYKDDDDK antibody and SA-XL665 mixture (each 1:100 dilution in binding buffer) was added to each reaction system and incubated for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection. )
SDS-PAGE (Recombinant p53 (TP53) protein gel 10% SDS-PAGE Coomassie staining MW: 44.9 kDa Purity: ? 95% )
Application Data (HTRF assay for recombinant AKT2 protein activity 1 uM STK S3 substrate was incubated with different concentrations AKT2 protein in a 10 ul reaction system for 1 hour. The 10 ul detection reagents were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature, and HTRF KinEASE STK assay was used to detect the enzymatic activity.)
Application Data (HTRF assay for recombinant AKT2 protein activity 1 uM STK S3 substrate was incubated with different concentrations AKT2 protein in a 10 ul reaction system for 1 hour. The 10 ul detection reagents were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature, and HTRF KinEASE STK assay was used to detect the enzymatic activity.)
SDS-PAGE (Recombinant AKT2 protein gel 10% SDS-PAGE Coomassie staining MW: 60.6 kDa Purity: ?90%)
SDS-PAGE (Streptavidin pull down assay for Recombinant Mononucleosomes H3.1 (K4M) - biotin 24 ug biotinylated mononucleosomes were incubated with 10 ul streptavidin beads for 1hr at 4 degree C. Streptavidin beads were washed 3 times with 1 ml binding buffer. Then the beads were added 60 ul 2×SDS loading buffer and boiled for 10 min at 95 degree C. 2.4 ul samples were loaded and run on a 12.5% SDS-PAGE gel and stained by Commassie bule. * indicates streptavidin. The SDS-PAGE gel result showed that >80% of biotinylated mononucleosomes were pulled down by streptavidin beads.)
SDS-PAGE (Recombinant Mononucleosomes H3.1 (K4M) - biotin 12.5% SDS-PAGE gel with Coomassie Blue staining MW: 108 kDa Purity: >95%)
Application Data (Recombinant Mononucleosomes H3.1 (K4M) - biotin DNA gel Recombinant Mononucleosomes H3.1 (K4M) - biotin were run on a 2% agarose gel and stained with ethidium bromide. Lane 1: DNA marker. Lane 2: 601 DNA which was used for assembly of nucleosome. Lane 3: Intact mononucleosomes H3.1 (K4M) - biotin. Intact mononucleosomes H3.1 (K4M) - biotin migrated much higher than free 601 DNA. The agarose gel shows that almost all of 601 DNA wrapped histone octamers to form nucleosomes.)
Application Data (HTRF for IGF2BP3 activity 1 uM ACTB zipcode ssDNA (1212-1313) was incubated with different concentrations of IGF2BP3 protein in a 10 ul reaction system containing 50 mM HEPES-NaOH pH 7.5, 0.1% BSA for 1 hour, then 10 ul anti-DYKDDDDK antibody and SA-XL665 mixture (1:100 dilution in the same buffer) was added to each reaction system and incubated for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Application Data (HTRF for IGF2BP3 activity 1 uM ACTB zipcode ssDNA (1212-1313) was incubated with different concentrations of IGF2BP3 protein in a 10 ul reaction system containing 50 mM HEPES-NaOH pH 7.5, 0.1% BSA for 1 hour, then 10 ul anti-DYKDDDDK antibody and SA-XL665 mixture (1:100 dilution in the same buffer) was added to each reaction system and incubated for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
SDS-PAGE (Recombinant IGF2BP3 protein gel 10% SDS-PAGE with Coomassie blue staining MW: 65 kDa Purity: >85%)
SDS-PAGE (Streptavidin pull down assay for Recombinant Mononucleosomes H3.1 (R26C) – biotin 24 ug biotinylated mononucleosomes were incubated with 10 ul streptavidin beads for 1 hr at 4 degree C. Streptavidin beads were washed 3 times with 1 ml binding buffer. The beads were added 60 ul 2×SDS loading buffer and boiled for 10 min at 95 degree C. 2.4 ul samples were loaded and run on a 12.5% SDS-PAGE gel stained with Coomassie blue. The SDS-PAGE gel shows that >88% of biotinylated mononucleosomes were pulled down by streptavidin beads.)
Application Data (Recombinant Mononucleosomes H3.1 (R26C) - biotin DNA gel Recombinant Mononucleosomes H3.1 (R26C) - biotin were run on a 2% agarose gel and stained with ethidium bromide. Lane 1: DNA marker. Lane 2: 601 DNA which was used for assembly of nucleosomes. Lane 3: Intact mononucleosomes H3.1 (R26C) - biotin. Intact mononucleosomes H3.1 (R26C) - biotin migrated much higher than free 601 DNA. The agarose gel shows that almost all of 601 DNA wrapped histone octamers to form nucleosomes.)
SDS-PAGE (Recombinant Mononucleosomes H3.1 (R26C) – biotin 12.5% SDS-PAGE with Coomassie blue staining MW: 108 kDa Purity: >95%)
SDS-PAGE (Streptavidin pull down assay for Recombinant Mononucleosomes H3.3 (K4I) – biotin 24 ug biotinylated mononucleosomes were incubated with 10 ul streptavidin beads for 1hr at 4 degree C. Streptavidin beads were washed 3 times with 1 ml binding buffer. The beads were added to 60 ul 2×SDS loading buffer and boiled for 10 min at 95 degree C. 2.4 ul samples were loaded on a 12.5% SDS-PAGE gel and stained by Commassie blue. The SDS-PAGE gel result showed that almost all of biotinylated mononucleosomes were pulled down by streptavidin beads.)
Application Data (Recombinant Mononucleosomes H3.3 (K4I) - biotin DNA gel Recombinant Mononucleosomes H3.3 (K4I) - biotin were run on a 2% agarose gel and stained with ethidium bromide. Lane 1: DNA marker. Lane 2: Free 601 DNA which was used for assembly of nucleosome. Lane 3: Intact mononucleosomes H3.3 (K4I) - biotin. Intact mononucleosomes H3.3 (K4I) - biotin migrated much higher than free 601 DNA. The agarose gel shows that almost all of 601 DNA wrapped histone octamers to form nucleosomes.)
SDS-PAGE (Recombinant Mononucleosomes H3.3 (K4I) – biotin 12.5% SDS-PAGE with Coomassie blue staining MW: 108 kDa Purity: >92%)
Application Data (HTRF assay for MAPKAPK3 activity 1 uM STK S1 substrate was incubated with different concentrations of MAPKAPK3 protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, and 100 uM ATP for 1 hour. Then 10 mul detection reagents containing 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 MAPKAPK3 protein 10% SDS-PAGE with Coomassie blue staining MW: 44 kDa Purity: >90%)
Application Data (AMP-Glo assay for UBE2C activity 7.9uM ubiquitin, 63 nM UBA1 and 25uM ATP were incubated with different concentrations of UBE2C in 10ul reaction system containing 40 mM Tris-HCl pH 7.4, 20 mM MgCl2, 0.5 mM DTT, 0.1 mg/ml BSA at 37? for 1 hour. 10ul of AMP-Glo Reagent I was added to the reaction and incubated for 1 hour at room temperature. Then 20ul of AMP-Glo Detection Solution was added and luminescence was read after another 30 min incubation.)
SDS-PAGE (Recombinant UBE2C protein gel. UBE2C protein was run on a 12.5% SDS-PAGE gel and stained with Coomassie Blue. MW: 21.82kDa Purity: >90%)
ELISA (ELISA for PARG activity 25uM NAD-Biotin and Actived DNA were added into ELISA plate (coated with histone H2A and H2B mixture) with PARP1 in ADPR Buffer and incubated for 1 hour at room temperature. After washing, different concentrations of PARG were added into each well and incubated in reaction buffer for 1 hour at room temperature. Following Streptavidin-HRP and ECL incubation, the plate was read in a luminometer or microtiter-plate reader.)
ELISA (ELISA for PARG activity 25uM NAD-Biotin and Actived DNA were added into ELISA plate (coated with histone H2A and H2B mixture) with PARP1 in ADPR Buffer and incubated for 1 hour at room temperature. After washing, different concentrations of PARG were added into each well and incubated in reaction buffer for 1 hour at room temperature. Following Streptavidin-HRP and ECL incubation, the plate was read in a luminometer or microtiter-plate reader.)
SDS-PAGE (Recombinant PARG protein gel. PARG protein was run on a 10% SDS-PAGE gel and stained with Coomassie Blue. MW: 113.63kDa Purity: >75%)
Infected Trichoplusia ni cells are lysed and centrifuged and then the soluble extract containing the VLPs is dialyzed against Phosphate Buffered Saline.
>95% pure (10% PAGE coomassie staining). GS-4B Sepharose Affinity Purification.
Pricing
What Are Recombinant Proteins?
Recombinant proteins are purified laboratory reagents produced through genetic engineering. A specific gene of interest is inserted into a host organism, such as mammalian, bacterial, yeast, or insect cells, which then expresses the protein in a controlled environment.
The recombinant process utilized to generate the recombinant proteins in our catalog provides precise control over sequence modifications, expression levels, and large-scale production tailored to experimental needs. These recombinants are widely used in research to investigate protein-protein interactions, enzyme activities, receptor-ligand binding, and cellular responses. Additionally, recombinant proteins serve as standards or controls in immunostaining assays and support cell growth and differentiation in culture systems, particularly in immunology, oncology, and structural biology studies.
Common Applications of Recombinant Proteins
Studying protein-protein and protein-DNA interactions
Functional assays to study biological pathways
Standard curves in ELISA and other quantitative assays
Use as antigens for antibody production
Development and screening of therapeutic drugs
Biomarker discovery and validation
Cell signaling and immune response studies
Vaccine research and development
Key Features of AAA Biotech’s Recombinant Proteins
High Purity: Most proteins are purified to ≥95% using affinity chromatography and other validated techniques.
Biological Activity: If functional activity is tested and confirmed for a given protein, it will be noted directly on the product page.
Multiple Expression Systems: Available in E. coli, HEK293, CHO, yeast, and insect cells to match your assay requirements.
Custom Tags Available: His-tag, GST, FLAG, and Fc fusion options for easy purification and detection.
Wide Range of Targets: Cytokines, growth factors, enzymes, receptors, signaling proteins, and more.
Validated Consistency: Lot-to-lot consistency ensured through rigorous QC protocols.
Flexible Quantities: Available in various pack sizes to suit different experimental needs.
Ready-to-Use Format: Lyophilized or liquid formulations that are easy to reconstitute and use.
Why Buy Recombinant Proteins from AAA Biotech?
At AAA Biotech, we are committed to supporting the research community with recombinant proteins that offer exceptional performance and reliability. Our proteins are produced using industry-standard methods and are validated to meet the needs of academic, pharmaceutical, and biotechnology laboratories.
With competitive pricing, global shipping, and dedicated technical support, AAA Biotech makes it simple and convenient to source the high-quality recombinant proteins your work depends on.
FAQ
1. How are AAA Biotech recombinant proteins validated?
Each batch undergoes stringent quality control checks, including SDS-PAGE analysis, endotoxin testing (for select products), and activity assaying (for select products). Certificates of Analysis are provided with every product.
2. Are your proteins suitable for therapeutic development or only research?
AAA Biotech recombinant proteins are strictly for research-use only and are not intended for diagnostic or therapeutic purposes in humans or animals.
3. What types of expression systems do you use for recombinant protein production?
The production labs use a variety of expression platforms, including bacterial (E. coli), yeast, insect (baculovirus), and mammalian (HEK293, CHO) systems. The expression system used depends on the complexity and intended function/use of the protein.
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