The synthesized peptide derived from human Beta-Actin (1-50aa) is used as the immunogen to immunize the mouse. To generate the ACTB monoclonal antibody, B cells isolated from the immunized mouse are fused with myeloma cells to form hybridoma cells. The hybridoma cells that produce the ACTB antibody are then selected and cultured, and the ACTB monoclonal antibody is purified from the mouse ascites using protein A affinity chromatography. The purity of this ACTB monoclonal antibody is greater than 95%. It is highly specific to the ACTB protein from four species including human, mouse, rat, and rabbit, and can be used in five assays including ELISA, WB, IHC, IF, and FC.

ACTB is one of the most abundant cytoskeletal proteins found in eukaryotic cells. Specifically, ACTB is involved in cell motility and cytoskeletal organization. It is one of the most widely used housekeeping genes in molecular biology and is often used as a reference gene in gene expression studies. ACTB is also commonly used as a loading control in WB experiments.

CUSABIO immunized the mouse with the recombinant GFP protein to get the splenocytes that secret the GFP antibody. The GFP-producing splenocytes were subsequently fused with myeloma cells to form hybridomas, which were inoculated into the abdominal cavity of mice. The mouse ascites was collected and purified to get the monoclonal anti-GFP antibody. Following purification through protein A, the purity of the monoclonal GFP antibody is more than 95%. It is matched with the mouse IgG2bisotype. And it targets the GFP tag in ELISA, WB, IF, IP, and FC applications and reacts with the GFP protein from all species.

Green fluorescent protein (GFP) is a protein that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range. For this reason, GFP is used as a fluorescent protein reporter to determine the distribution and quantity of a particular target biomolecule both in vitro and in vivo, in conjunction with fluorescence microscopy techniques.

The monoclonal TUBB antibody is secreted from the hybridoma formed by the fusion of myeloma cells and splenocytes from mice immunized with the GAGNNWAKGHYTEGA synthetic peptide conjugated to KLH. It is purified from mouse ascites through protein A, and its purity reaches over 95%. This unconjugated TUBB monoclonal antibody is matched with the mouse IgG2b isotype. It has been tested for use in ELISA, WB, IHC, IF, FC, and IP applications and can detect the TUBB protein from human, mouse, rabbit, and rat species.

The TUBB protein is responsible for the stability and dynamic properties of microtubules. Microtubules are involved in a wide range of cellular processes, including cell division, cell motility, intracellular transport, and maintenance of cell shape. TUBB is required for proper microtubule function. TUBB is also the target of several anti-cancer drugs, which bind to microtubules and disrupt their function, leading to cell death.

The glutathione S transferase (GST) monoclonal antibody is secreted from the hybridoma formed by the fusion of mouse myeloma cells and splenocytes from mice immunized with the recombinant GST protein. It is purified from mouse ascites through protein A, and its purity reaches over 95%. This unconjugated GST monoclonal antibody is matched with the mouse IgG2b isotype. It is recommended for use in several scientific applications, including ELISA, WB, IF, FC, and IP applications, and can detect the GST tag from all species.

GST is a 26 kDa protein that naturally occurs in eukaryotic cells. GSTs can catalyze the binding of exogenous substances to glutathione (GSH), thereby detoxifying many environmental toxins including chemotherapy drugs, residual drugs, herbicides and carcinogens. Many researchers integrate GST DNA sequences into expression vectors to produce fusion proteins with GST tags. GST can quickly fold and be stable and has good solubility, so it can promote the expression and dissolution of the fusion protein. In addition, the binding between GST and its substrate GSH can also be used for protein purification and detection. At present, GST-tagged proteins are used in recombinant protein expression, affinity purification, antigen immunity, vaccine research, and pull-down, affinity chromatography and ELISA in a variety of research technology experiments.

This Histone H3 monoclonal antibody production began with immunization of a mouse with KDIQLARRIRGERA synthetic peptide conjugate to KLH. Several weeks after immunization, spleen cells were harvested. B cells in the spleen produced the Histone H3 antibody but could not grow in culture. The spleen cells were fused with cells of a myeloma line. The myeloma cells could not produce antibodies, but they would immortally grow in culture. The two cells were fused together to produce a hybrid cell that could be used to make the desired Histone H3 antibody. This Histone H3 monoclonal antibody was purified by Protein A and validated in ELISA, WB, IHC, IP.

The V5-Tag monoclonal antibody is generated using recombinant the GKPIPNPLLGLDST synthetic peptide conjugate to KLH as the immunogen, with B cells from immunized mice being fused with myeloma cells to create hybridomas. The hybridoma cells that produce the V5-Tag antibody are screened and cultured, and the V5-Tag monoclonal antibody is purified from the mouse ascites using protein G affinity chromatography, with a purity of over 95%. This unconjugated IgG1 antibody is suitable for detecting all V5-Tagged proteins in ELISA, WB, IF, IP, and FC assays.

The V5-tag is a short peptide sequence (GKPIPNPLLGLDST) that is commonly added to recombinant proteins to facilitate their detection and purification. It is often fused to a protein of interest using genetic engineering techniques. The V5-tag is widely used in the study of protein-protein interactions, protein localization, and protein trafficking within cells.

The mouse is immunized with synthetic peptide GLNDIFEAQKIEWHE to obtain the B cells. Fusing mouse B cells with myeloma cells to obtain hybridomas, selecting the hybridoma cell line that produces the Avi-Tag antibody, and then culturing the selected hybridoma in the mouse abdominal cavity. The Avi-Tag monoclonal antibody is from the mouse ascites using protein G affinity chromatography, resulting in a purity of over 95%. This unconjugated IgG2a antibody is ideal for detecting the all Avi-Tagged proteins in ELISA, WB, and IP applications. The Avi-Tag is a short peptide sequence (GLNDIFEAQKIEWHE) that can be genetically encoded onto a protein of interest.

The Avi-Tag sequence is recognized by the biotin ligase enzyme BirA, which covalently attaches biotin to a specific lysine residue within the Avi-Tag sequence. The biotinylated protein can then be easily purified or detected using streptavidin-linked reagents, which bind specifically to biotin with high affinity. This makes the Avi-Tag a useful tool for studying protein localization, interaction, and function.