Phospho-VASP (S238) Polyclonal Antibody, 100 µg, (ATB-P0272)

Description

Background:

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:

References:

1. 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.
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2. 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.
3. 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.
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   Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC]

   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Substantia nigra.

4. 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.
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   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases

   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

5. 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.
6. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.
   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
   Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2. Tissue: Platelet.
7. Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization.
   Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P., Walter U.
   Genomics 36:227-233(1996) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-380.
8. cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets.
   Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.
   J. Biol. Chem. 269:14509-14517(1994) [PubMed] [Europe PMC] Cited for: PROTEIN SEQUENCE OF 143-164; 235-244 AND 267-285, PHOSPHORYLATION AT SER-157; SER-239 AND THR-278 BY PRKG1.
9. Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition.
   Horstrup K., Jablonka B., Honig-Liedl P., Just M., Kochsiek K., Walter U.
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10. The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins.
    Reinhard M., Giehl K., Abel K., Haffner C., Jarchau T., Hoppe V., Jockusch B.M., Walter U.
    EMBO J. 14:1583-1589(1995) [PubMed] [Europe PMC] Cited for: INTERACTION WITH ACTG1 AND PFN1.