ARG65788

anti-VASP antibody

anti-VASP antibody for ICC/IF,IHC-Formalin-fixed paraffin-embedded sections,Western blot and Human,Mouse,Rat

Overview

Product Description Rabbit Polyclonal antibody recognizes VASP
Tested Reactivity Hu, Ms, Rat
Predict Reactivity Bov, Dog
Tested Application ICC/IF, IHC-P, WB
Specificity Recognizes endogenous levels of VASP protein.
Host Rabbit
Clonality Polyclonal
Isotype IgG
Target Name VASP
Antigen Species Human
Immunogen KLH-conjugated synthetic peptide around the center region of Human VASP.
Conjugation Un-conjugated
Alternate Names VASP; Vasodilator-stimulated phosphoprotein

Application Instructions

Application Suggestion
Tested Application Dilution
ICC/IF1:100 - 1:500
IHC-P1:100 - 1:200
WB1:500 - 1:1000
Application Note IHC-P: Antigen Retrieval: Sodium citrate buffer (pH 6.0)
* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.

Properties

Form Liquid
Purification Affinity purification with immunogen.
Buffer Aqueous liquid (pH 7.3), 0.42% Potassium phosphate, 0.87% Sodium chloride, 0.01% Sodium azide and 30% Glycerol.
Preservative 0.01% Sodium azide
Stabilizer 30% Glycerol
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 22323 Mouse VASP

GeneID: 7408 Human VASP

Swiss-port # P50552 Human Vasodilator-stimulated phosphoprotein

Swiss-port # P70460 Mouse Vasodilator-stimulated phosphoprotein

Gene Symbol VASP
Gene Full Name vasodilator-stimulated phosphoprotein
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]
Function 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. [UniProt]
Calculated MW 40 kDa
PTM Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG/PRKG1, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239. Phosphorylation at Ser-157 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-322 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239. Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239.