Phospho-VASP (S157) Polyclonal Antibody, 100µg, (ATB-P0271)
$238.00
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Description
Background:
Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. [provided by RefSeq, Jul 2008]
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.
Product datasheet:
Overview | |
| Product Description | Phospho-VASP (S157) Polyclonal Antibody, 100µg, (ATB-P0271) |
| Image | ![]() |
| Species Reactivities | Human,Mouse,Rat,Monkey |
| Immunogen | Synthesized peptide derived from human VASP around the phosphorylation site of S157. |
Properties | |
| Form | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. |
| Storage Instructions | -20°C/1 year |
| Clonality | Polyclonal |
References:
- Reconstitution of actin-based motility by vasodilator-stimulated phosphoprotein (VASP) depends on the recruitment of F-actin seeds from the solution produced by cofilin. Siton O, et al. J Biol Chem, 2014 Nov 7. PMID 25246528
- Role of serum vaspin in progression of type 2 diabetes: a 2-year cohort study. Jian W, et al. PLoS One, 2014. PMID 24732788 Free PMC Article
- Matrine inhibits the adhesion and migration of BCG823 gastric cancer cells by affecting the structure and function of the vasodilator-stimulated phosphoprotein (VASP). Zhang JW, et al. Acta Pharmacol Sin, 2013 Aug. PMID 23685951 Free PMC Article
- Natriuretic peptides induce weak VASP phosphorylation at Serine 239 in platelets. Borgognone A, et al. Platelets, 2014. PMID 23469931 Free PMC Article
- High on-treatment platelet reactivity assessed by various platelet function tests: is the consensus-defined cut-off of VASP-P platelet reactivity index too low? Jeong YH, et al. J Thromb Haemost, 2012 Mar. PMID 22212857
- Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP.
Haffner C., Jarchau T., Reinhard M., Hoppe J., Lohmann S.M., Walter U.
EMBO J. 14:19-27(1995) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-32; 87-96; 140-154; 255-282 AND 297-322, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POSSIBLE FUNCTION. Tissue: Promyelocyte. - Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes.
Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L., Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F.
J. Cell Biol. 144:1245-1258(1999) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH L.MONOCYTOGENES ACTA. - Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Substantia nigra.
- Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal lung, Fetal spleen and Skin.


| size | chest(in.) | waist(in.) | hips(in.) |
|---|---|---|---|
| XS | 34-36 | 27-29 | 34.5-36.5 |
| S | 36-38 | 29-31 | 36.5-38.5 |
| M | 38-40 | 31-33 | 38.5-40.5 |
| L | 40-42 | 33-36 | 40.5-43.5 |
| XL | 42-45 | 36-40 | 43.5-47.5 |
| XXL | 45-48 | 40-44 | 47.5-51.5 |





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