TAP Tag Monoclonal Antibody

The TAP tag (Tandem Affinity Purification tag) is a sophisticated and powerful tool extensively utilized in molecular biology for the identification and characterization of protein complexes in their native, near-physiological state. The classic TAP system typically consists of two distinct affinity tags—such as Staphylococcus aureus Protein A and a Calmodulin Binding Peptide (CBP)—separated by a protease cleavage site (e.g., TEV protease). This design allows for a highly stringent, two-step affinity purification process, effectively isolating the target "bait" protein along with its associated "prey" proteins while minimizing non-specific background.

The Mouse Anti-TAP-Tag Monoclonal Antibody (CSB-MA000286, IgG isotype) is specifically engineered to provide high-affinity, monospecific recognition of this tandem affinity tag. Produced via robust hybridoma technology using a recombinant TAP tag protein as the immunogen, this antibody guarantees exceptional specificity, lot-to-lot consistency, and reliable performance in complex sample matrices.

Validated for both ELISA and Western Blot (WB) applications, the antibody exhibits outstanding sensitivity and a high binding affinity. As demonstrated in the Western Blot analysis, the antibody successfully detects the TAP recombinant protein at a working dilution of 1:5,000. The distinct, crisp band observed on the membrane underscores the antibody's excellent immunoreactivity and superior signal-to-noise ratio, making it a highly cost-effective reagent for routine laboratory use.

This antibody is an indispensable tool for proteomic researchers. It serves as a critical reagent for verifying successful TAP fusion protein expression, assessing protein molecular weight, and providing a reliable handle for downstream tandem affinity purification workflows. With its proven performance, the TAP-Tag Monoclonal Antibody ensures dependable, high-quality results to support cutting-edge research in protein-protein interaction mapping and complex network analysis.