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10ng of Paxillin recombinant protein was resolved by electrophoresis, transferred to nitrocellulose, and probed with anti-Paxillin antibody (Clone PAX227). Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and chemiluminescence detection.
Recombinant full-length human paxillin produced in E. coli with >70% purity as determined by Comassie Blue staining of an SDS-PAGE gel. Paxillin (also known as peroxisomal membrane protein 3) is a cytoplasmic protein with LIM metal-binding repeat homology and LIM domains. Endogenous paxillin has three isoforms designated as α, β, γ; with approximate molecular weights of 68 kD. Paxillin is localized to actin-membrane attachment at sites of cell adhesion to extracellular matrix (focal adhesion). This protein undergoes cell adhesion-dependent tyrosine phosphorylation. Paxillin has been shown to interact with FAK, vinculin, src, Crk, p210BRC / ABL, talin, and integrin-β1.
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