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.
Application Data (Recombinant Mononucleosomes H3.1 (K18M) DNA gel Recombinant Mononucleosomes H3.1 (K18M) 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 (K18M). Intact mononucleosomes H3.1 (K18M) migrated much higher than free 601 DNA. The agarose gel shows that almost all of 601 DNA wrapped histone octamers to form nucleosomes.)
WB (Western Blot) (Western blot assay for Recombinant Mononucleosomes H3.1 (K4I) 2 ug Recombinant Mononucleosomes H3.1 (K4I) were incubated with 0 or 10 nM MLL2 Complex respectively in reaction buffer containing 50 mM Tris-HCl pH 8.6, 0.02% Triton X-100, 2 mM MgCl2, 1 mM TCEP and 50 uM SAM for 3 hr at room temperature. Half of the reactions were run on a 12.5% SDS-PAGE gel and detected with H3K4me2 antibody and anti-H4 antibody , respectively. H4 was detected as loading control. Recombinant Mononucleosomes H3.1 and Histone H3.1 was used as a positive control. The result shows that no H3K4me2 products were generated when Mononucleosomes H3.1 (K4I) were incubated with MLL2 Complex.)
Application Data (Recombinant Mononucleosomes H3.1 (K4I) DNA gel Recombinant Mononucleosomes H3.1 (K4I) 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 (K4I). Intact Mononucleosomes H3.1 (K4I) 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 (SDS-PAGE analysis (15%) of 2 uL of recombinant ZEBRA. Purity is >98% as determined by gel electrophoresis.)
ELISA (Titration Curve by an ELISA Assay. The titer has been suggested in reference to an "in-house" ELISA kit performed at the lab over the first lot obtained. Each end user should carry out their own titration for their particular application. In this plot, the optical density at 450/620 nm for positive (blue) and negative (gray) IgG sera are compared for each concentration of the recombinant antigen. An appropriate statistical test of significance for the comparison of means between both groups, the Welch's test, is employed. Eligible concentrations for the use of the antigen should present statistically significant differences between positive and negative sera. This happens when the intervals at the top do not overlap and, equivalently, when the value at the bottom is below 0.05. In the present figure, all p-values are below 0.05 and thus the intervals do not overlap. Therefore, any of the showed concentrations can be used to distinguish between positive and negative sera.)
Standard Curve (Sample) (In this plot, the optical density at 450/620 nm for positive (blue) and negative (gray) IgG sera are compared for each concentration of the recombinant antigen. An appropriate statistical test of significance for the comparison of means between both groups, the Welch's test, is employed. Eligible concentrations for the use of the antigen should present statistically significant differences between positive and negative sera. This happens when the intervals at the top do not overlap and, equivalently, when the p-value at the bottom is below 0.05. In the present figure, all p-values are below 0.05 and thus the intervals do not overlap. Therefore, any of the showed concentrations can be used to distinguish between positive and negative sera.)
SDS-PAGE (Purity control in SDS-PAGE: 15%)
Application Data (This protein does not contain any Trp residues. Experience shows that this could result in more than 10% error in the computed extinction coefficient Therefore, we have measured the protein concentration by using the colorimetric assay based on the interaction between Coomassie brilliant blue and the arginine and aromatic residues (Bradford Method) and its maximum absorption shifts from 470 nm to 595 nm. The standard curve was performed with the protein BSA. 40 μl of the protein were analysed.)
SDS-PAGE (Figure 3. B7H6 protein is highly expressed on the surface of Expi293 cell membrane. Flow cytometry analysis with 2ug/ml Human NKp30 Protein, hFc Tag (AAA47240) on Expi293 cells transfected with human B7H6 (Blue histogram) or Expi293 transfected with irrelevant protein (Red histogram), and Isotype antibody on Expi293 transfected with irrelevant protein (Orange histogram).)
ELISA (Figure 3. B7H6 protein is highly expressed on the surface of Expi293 cell membrane. Flow cytometry analysis with 2ug/ml Human NKp30 Protein, hFc Tag (AAA47240) on Expi293 cells transfected with human B7H6 (Blue histogram) or Expi293 transfected with irrelevant protein (Red histogram), and Isotype antibody on Expi293 transfected with irrelevant protein (Orange histogram).)
ELISA (Biotinylated Human TIGIT Protein ELISA DataImmobilized Biotinylated Human TIGIT, His Tag at 0.5?g/ml (100?l/well) on the streptavidin precoated plate (5?g/ml). Dose response curve for Human CD155, hFc Tag with the EC50 of 8.7ng/ml determined by ELISA.)
Application Data (Biotinylated Human TIGIT Protein SEC-HPLCThe purity of Biotinylated Human TIGIT is greater than 95% as determined by SEC-HPLC.)
Tris-Bis-PAGE (Biotinylated Human TIGIT Protein Tris-Bis PAGEBiotinylated Human TIGIT on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.)
Application Data (Biotinylated Mouse MSLN/Mesothelin Protein (Primary Amine Labeling) SEC-HPLCThe purity of Biotinylated Mouse MSLN is greater than 95% as determined by SEC-HPLC.)
Tris-Bis-PAGE (Biotinylated Mouse MSLN/Mesothelin Protein (Primary Amine Labeling) Tris-Bis PAGEBiotinylated Mouse MSLN on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.)
WB (Western Blot) (Western blot assay for Recombinant Mononucleosomes H3.1 (K27M) 2 ug Recombinant Mononucleosomes H3.1 (K27M) were incubated with 0 or 100 nM PRC2 respectively in reaction buffer containing 50 mM Tris-HCl pH 8.6, 0.02% Triton X-100, 2 mM MgCl2, 1 mM TCEP and 50 ?M SAM for 3 hr at room temperature. Half of the reactions were run on a 12.5% SDS-PAGE gel and detected with anti-H3K27me1 antibody . Mononucleosomes H3.1 were used as a control. The Western Blot result shows that only the H3K27 of mononucleosomes H3.1 can be methylated by PRC2.)
SDS-PAGE (Recombinant Mononucleosomes H3.1 (K27M) 12.5% SDS-PAGE gel, stained with Coomassie Blue MW: 108 kDa Purity: >92%)
Application Data (Recombinant Mononucleosomes H3.1 (K27M) DNA gel Recombinant Mononucleosomes H3.1 (K27M) 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 (K27M). Intact mononucleosomes H3.1 (K27M) 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 (Streptavidin pull down assay for Recombinant Mononucleosomes H3.3 (K9M) – 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 almost all of the biotinylated mononucleosomes were pulled down by streptavidin beads.)
Application Data (Recombinant Mononucleosomes H3.3 (K9M) - biotin DNA gel Recombinant Mononucleosomes H3.3 (K9M) - 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 (K9M) - biotin. Intact mononucleosomes H3.3 (K9M) - 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 (K9M) – biotin 12.5% SDS-PAGE with Coomassie blue staining MW: 108 kDa Purity: >92%)
HBsAg adr, Hepatitis B Surface Antigen adr subtype, CHO
Applications
Western Blot
Purity
> 95% (by SDS-PAGE) Purified by proprietary chromatographic technique
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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