Anti-Paxillin Antibody

Paxillin is a 68 kDa focal adhesion phosphoprotein that acts as a scaffold at integrin-based adhesion sites, linking the actin cytoskeleton to the extracellular matrix and recruiting signaling effectors such as FAK, Src, and Crk. Phosphorylation of paxillin on tyrosine, serine, and threonine residues regulates its role in cell spreading, migration, and mechanical force transduction, making it a frequently used marker in cell adhesion and motility research.

This unconjugated rabbit polyclonal antibody from Antibodies.com detects endogenous paxillin in human, mouse, and rat samples. It is supplied as a 100 µl aliquot and is validated for Western blot analysis of the native protein in cell and tissue lysates, as well as ELISA-based immunoassays. The polyclonal format increases the likelihood of recognizing multiple epitopes, including both phosphorylated and non-phosphorylated forms under denaturing conditions.

Researchers use anti-paxillin antibodies to characterize focal adhesion dynamics during epithelial-mesenchymal transition, tumor cell invasion, fibroblast mechanotransduction, and developmental morphogenesis. The 100 µl volume provides enough reagent for multiple immunoblotting experiments paired with standard chemiluminescent or chromogenic detection workflows.