MBP Monoclonal Antibody
Description
The MBP monoclonal antibody is produced by immunizing mice with the MBP-Tag fusion protein and then fusing B cells isolated from the immunized mice with myeloma cells to create hybridomas. After screening, the best hybridoma cell line is cultured in the mouse abdominal cavity. The MBP monoclonal antibody is purified from the mouse ascites using protein G affinity chromatography to ensure a purity of over 95%. This unconjugated IgG2a antibody is ideal for detecting MBP-tagged proteins in ELISA and WB applications.
MBP is a cytoplasmic protein that binds specifically to maltose and other sugar molecules. It is commonly used as a fusion partner for recombinant protein expression and purification, allowing for efficient purification of the fused protein using immobilized metal ion affinity chromatography (IMAC) or amylose resin. MBP has also been shown to have chaperone activity and can enhance the solubility and stability of fusion proteins. In addition, MBP has been used as a tool in studies of protein-protein interactions and protein folding.
Product Specs
The MBP monoclonal antibody is generated by immunizing mice with the MBP-Tag fusion protein. Subsequently, B cells isolated from the immunized mice are fused with myeloma cells to create hybridomas. After a rigorous screening process, the most productive hybridoma cell line is cultured in the mouse abdominal cavity. The MBP monoclonal antibody is purified from mouse ascites using protein G affinity chromatography, ensuring a purity exceeding 95%. This unconjugated IgG2a antibody is optimally suited for detecting MBP-tagged proteins in ELISA and Western blotting applications.
MBP, a cytoplasmic protein, exhibits a high affinity for maltose and other sugar molecules. Its widespread use as a fusion partner for recombinant protein expression and purification stems from its ability to facilitate efficient purification through immobilized metal ion affinity chromatography (IMAC) or amylose resin. Furthermore, MBP has been shown to possess chaperone activity, enhancing the solubility and stability of fusion proteins. Additionally, MBP serves as a valuable tool in investigating protein-protein interactions and protein folding mechanisms.
