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Vasodilator-Stimulated phosphoprotein (VASP) (AA 248-379) antibody

Details for Product No. ABIN967977
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Antigen
Synonyms vasp, MGC80889, wu:fb23b04, wu:fk84g05, zgc:110347, si:dkey-113g17.1, si:ch211-202c21.1, DDBDRAFT_0188463, DDBDRAFT_0229340, DDB_0188463, DDB_0229340, VASP
Epitope
AA 248-379
(46), (25), (19), (12), (8), (7), (7), (4), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(193), (134), (108), (36), (24), (3), (2)
Host
Mouse
(175), (19)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(7), (7), (4), (3), (3), (3), (3), (3), (3), (3), (3), (2), (1), (1), (1)
Application
Western Blotting (WB), Immunofluorescence (IF)
(158), (74), (56), (34), (30), (25), (16), (13), (9), (2), (1), (1)
Pubmed 5 references available
Quantity 150 µg
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Catalog No. ABIN967977
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Immunogen Human VASP - 379
Clone BE10
Isotype IgG1
Cross-Reactivity Dog (Canine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name VASP
Background Vasodilator-stimulated phosphoprotein (VASP), a substrate for cAMP- and cGMP-dependent kinases, is associated with actin filaments, focal adhesions, and dynamic membrane regions. VASP is composed of several distinct domains: a central L-proline-rich domain contains a GPPPPP motif as a single copy and as a three-fold tandem repeat, as well as three conserved phosphorylation sites for cyclic nucleotide-dependent protein kinases (Ser157, Ser239, and Thr278). A C-terminal domain contains a repetitive mixed-charge cluster which is predicted to form an alpha-helix. The C-terminal domain appears to be responsible for anchoring at focal adhesion sites. VASP has been shown to be a ligand for profilins. Profilins bind to the poly-L-proline motifs of VASP and it is postulated that these two molecules act in concert to convey signal transduction to actin filament formation.
Molecular Weight 46 kDa
Research Area Signaling, Extracellular Matrix
Comment

Related Products: ABIN968536

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
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 -20 °C
Supplier Images
anti-Vasodilator-Stimulated phosphoprotein (VASP) (AA 248-379) antibody Western blot analysis of VASP on human endothelial cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-VASP.
anti-Vasodilator-Stimulated phosphoprotein (VASP) (AA 248-379) antibody (2) Immunoflurorescent staining on Human Endothelial cells.
anti-Vasodilator-Stimulated phosphoprotein (VASP) (AA 248-379) antibody (3) anti-Vasodilator-Stimulated phosphoprotein (VASP) (AA 248-379) antibody (Image 3)
Product cited in: Reinhard, Giehl, Abel et al.: "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins." in: The EMBO journal, Vol. 14, Issue 8, pp. 1583-9, 1995 (PubMed).

Haffner, Jarchau, Reinhard et al.: "Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP." in: The EMBO journal, Vol. 14, Issue 1, pp. 19-27, 1995 (PubMed).

Lawrence, Pryzwansky: "The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 166, Issue 9, pp. 5550-6, 2001 (PubMed).

Howe, Hogan, Juliano: "Regulation of vasodilator-stimulated phosphoprotein phosphorylation and interaction with Abl by protein kinase A and cell adhesion." in: The Journal of biological chemistry, Vol. 277, Issue 41, pp. 38121-6, 2002 (PubMed).

DeMali, Barlow, Burridge: "Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion." in: The Journal of cell biology, Vol. 159, Issue 5, pp. 881-91, 2002 (PubMed).

Validation Images
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