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Paxillin antibody (PXN) (pTyr31)

Details for Product anti-PXN Antibody No. ABIN967589, Supplier: Log in to see
Antigen
  • CG18061
  • CG18576
  • CG31794
  • CT40481
  • CT42454
  • DPaxillin
  • DPxn
  • DPxn37
  • Dmel\\CG31794
  • Dpax
  • DpaxA
  • PDLP
  • dPax
  • pax
  • PXN
  • LOC100220858
  • AW108311
  • AW123232
  • Pax
  • wu:fw71f12
Alternatives
anti-Human Paxillin antibody for Western Blotting
Epitope
pTyr31
60
48
25
24
20
17
14
13
9
7
7
7
7
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6
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4
4
4
4
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3
3
3
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human
366
166
152
25
6
3
3
2
1
1
1
1
1
Host
Mouse
334
47
2
Clonality (Clone)
Monoclonal ()
Conjugate
This Paxillin antibody is un-conjugated
7
7
7
7
5
5
5
5
5
5
5
5
2
2
2
1
1
Application
Western Blotting (WB)
290
101
91
58
47
46
26
22
8
8
4
2
2
1
1
1
Supplier
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Brand BD Pharmingen™
Clone 19-Paxillin
Isotype IgG1, kappa
Characteristics 1. Please refer to us for technical protocols.
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.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Paxillin (PXN Antibody Abstract)
Background A number of cytoskeletal proteins are tyrosine phosphorylated in Rous sarcoma virus-transformed chick embryo fibroblasts. One of these is the 68-kDa paxillin protein. Paxillin is a cytoskeletal component that localizes to the focal adhesions at the ends of actin stress fibers. It is also present in the focal adhesions of Madin-Darby canine kidney epithelial cells, but is absent from the cell adherens junctions of these cells. Paxillin purified from chicken gizzard migrates as a diffuse band on SDS-PAGE with molecular weight of 65-70 kDa. It binds to the rod domain of vinculin, another focal adhesion protein. Paxillin is a substrate for several tyrosine kinases such as src, FAK, and P210BCR/ABL, and the phosphorylation of paxillin on tyrosine 31 (Y31) is affected by conditions that change cell-cell adhesion. This is consistent with the possibility 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 an extracellular matrix-independent manner. Although paxillin was initially detected in fibroblasts, its phosphorylation may also be important during neurite extension.
The 19/Paxillin (Y31) monoclonal antibody recognizes the phosphorylated Y31 of activated paxillin.
Molecular Weight 68 kDa
Research Area Cancer, Extracellular Matrix
Pathways MAPK Signaling, EGFR Signaling Pathway
Comment

Related Products: ABIN968630, ABIN968536, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer Aqueous buffered solution containing ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Storage Comment Store undiluted at 4°C.
Supplier Images
Western Blotting (WB) image for anti-Paxillin antibody (PXN) (pTyr31) (ABIN967589) Western blot analysis of paxillin (pY31) in human endothelial cells. Lysates from con...
Product cited in: Nakamura, Yano, Uchida et al.: "Tyrosine phosphorylation of paxillin alpha is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells." in: The Journal of biological chemistry, Vol. 275, Issue 35, pp. 27155-64, 2000 (PubMed).

Leventhal, Feldman: "Tyrosine phosphorylation and enhanced expression of paxillin during neuronal differentiation in vitro." in: The Journal of biological chemistry, Vol. 271, Issue 11, pp. 5957-60, 1996 (PubMed).

Salgia, Li, Lo et al.: "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL." in: The Journal of biological chemistry, Vol. 270, Issue 10, pp. 5039-47, 1995 (PubMed).

Turner, Glenney, Burridge: "Paxillin: a new vinculin-binding protein present in focal adhesions." in: The Journal of cell biology, Vol. 111, Issue 3, pp. 1059-68, 1990 (PubMed).