Myc-Tag Monoclonal Antibody

The Myc tag, derived from the human proto-oncogene c-Myc, is one of the most ubiquitously utilized epitope tags in molecular biology and protein engineering. Comprising a short peptide sequence of 10 amino acids (EQKLISEEDL), the c-Myc tag is frequently fused to the N- or C-terminus of recombinant proteins. Its compact nature ensures that it rarely interferes with the natural folding, stability, or biological function of the target protein, making it an ideal choice for a wide range of applications, from bacterial expression to complex mammalian cell systems.

The Mouse Anti-c-Myc Monoclonal Antibody (CSB-MA000182, IgG isotype) is meticulously produced to provide high-affinity, monospecific recognition of this 10-amino-acid sequence. Produced via robust hybridoma technology using a synthetic peptide as the immunogen, this antibody guarantees exceptional specificity, lot-to-lot consistency, and minimal cross-reactivity with endogenous cellular components.

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 c-Myc recombinant protein at a working dilution of 1:2,000. The distinct, crisp band observed on the membrane, with no visible signs of degradation or background interference, underscores the antibody's excellent immunoreactivity and superior signal-to-noise ratio. This high titer and sensitivity make it an exceptionally cost-effective reagent for routine laboratory use.

This antibody is an indispensable tool for molecular biologists. It serves as a critical reagent for verifying successful c-Myc fusion protein expression, accurately assessing protein molecular weight, and providing a reliable handle for downstream biochemical assays and protein purification workflows. With its proven performance, the c-Myc Monoclonal Antibody ensures dependable, high-quality results to support research in protein engineering, gene function analysis, and structural biology.