Paxillin is involved in the integration of growth factor- and adhesion-mediated signal transduction pathways at focal adhesion sites. The LD motif of paxillin has been implicated in its binding to FAK, vinculin, and paxillin-kinase linker (p95PKL). p95PKL couples paxillin to a protein complex containing p21 GTPase-activated kinase (PAK), Nck, and the guanine nucleotide exchange factor, PIX. The sequence of p95PKL, highly homologous to human GIT1 and GIT2, predicts a structure that contains an N-terminal ARF-GAP domain containing a Zn2+ finger, three ankyrin repeats, an EF hand domain, and two IQ motifs. p95PKL binds to both paxillin and PIX and colocalizes with paxillin at focal adhesion sites. Overexpression of a paxillin LD4 deletion mutant in neuroblastoma cells inhibits insulin-like growth factor-1 mediated lamellipodia formation. Microinjection of this mutant into NIH3T3 cells has been reported to decrease migration into a wound. These alterations in cell motility are thought to involve PAK-mediated regulation of the actin cytoskeleton, since the LD4 motif of paxillin is required for p95PKL-dependent recruitment of PAK/PIX complexes to paxillin-containing focal adhesions sites. This antibody has been reported to recognize GIT1 and GIT2 proteins.
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注意事项：
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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