Technical Data
P3113-91V
Paxillin, phosphorylated (Tyr118) (PXN)
Description:
Paxillin is a focal adhesion protein and a substrate for several tyrosine kinases such as src, FAK, and p120BRC/ABL. The tyrosine phosphorylation of paxillin is affected by conditions that change cell-cell adhesion, consistent with the belief that paxillin is involved in the regulation of cell morphology. Additionally because of its SH3-binding domain, paxillin associates tightly with FAK and Crk in a manner that is independent of the extracellular matrix. Although paxillin was initially detected in fibroblasts, its phosphorylation may also be important during neurite extension during differentiation. Human paxillin gene is mapped to chromosome 12q24.31.

Applications:
Suitable for use in Western Blot and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 1:500-1:1000
Immunohistochemistry (paraffin): 1:50-1:100
Optimal dilutions to be determined by the researcher.

Positive Control:
HeLa cells

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
50ug-20°CBlue IceHumanRabbit
Concentration:
As reported
Immunogen:
Synthetic phosphopeptide corresponding to human Paxillin around the phosphorylation site of tyrosine 118 (H-V-YP-S-F).
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in PBS (without Mg2+ and Ca2+), pH 7.4, 150mM sodium chloride, 0.02% sodium azide, 50% glycerol.
Specificity:
Recognizes human Paxillin when phosphorylated at Tyr118. Species Crossreactivity: mouse and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. De, C. et al. Expt. Cell. Res. 230:233-243 (1997). 2. Hanks, SK. et al. Bioessays. 19:137-145 (1997). 3. Leventhal, PS. et al. J. Biol. Chem. 272:5214-5218 (1997).