anti-VASP pAb (IG-731)

AdipoGen Life Sciences
Product Code: AG-25T-0109
Product Group: Primary Antibodies
CodeSizePrice
AG-25T-0109-C02525 ug£440.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Antibody Clonality: Polyclonal
Regulatory Status: RUO
Target Species:
  • Human
  • Mouse
  • Porcine (pig)
Applications:
  • Immunocytochemistry (ICC)
  • Immunoprecipitation (IP)
  • Western Blot (WB)
Shipping:
-20°C
Storage:
-20°C

Further Information

Alternate Names/Synonyms:
Vasodilator-stimulated Phosphoprotein
Concentration:
250µg/ml
EClass:
32160000
Form (Short):
liquid
Formulation:
Liquid. In PBS containing 1mg/ml BSA and 0.02% sodium azide.
Handling Advice:
Avoid freeze/thaw cycles.
Immunogen:
Recombinant human VASP fused to a His-tag.
Long Description:
Polyclonal Antibody. Recognizes both the 46kDa (Ser157 dephospho-) and 50kDa (Ser157 phospho-) form of human, mouse and porcine VASP. Source: Rabbit. Applications: ICC, IP, WB. Liquid. In PBS containing 1mg/ml BSA and 0.02% sodium azide. VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein 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 proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.
NCBI, Uniprot Number:
P50552
Package Type:
Plastic Vial
Product Description:
VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein 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 proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.
Purity:
Antigen affinity purified.
Source / Host:
Rabbit
Specificity:
Recognizes both the 46kDa (Ser157 dephospho-) and 50kDa (Ser157 phospho-) form of human, mouse and porcine VASP.
Transportation:
Non-hazardous
UNSPSC Category:
Primary Antibodies
UNSPSC Number:
12352203
Use & Stability:
Stable for at least 1 year after receipt when stored at -20°C.

References

Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner: H. Hirata, et al.; J. Cell Sci. 121, 2795 (2008) | VASP is involved in cAMP-mediated Rac 1 activation in microvascular endothelial cells: N. Schlegel, & J. Waschke; Am. J. Physiol. Cell. Physiol. 296, C453 (2009) | Nitro-fatty acids reduce atherosclerosis in apolipoprotein E-deficient mice: T.K. Rudolph, et al.; Arterioscler. Thromb. Vasc. Biol. 30, 938 (2010) | The Eps8/IRSp53/VASP Network Differentially Controls Actin Capping and Bundling in Filopodia Formation: F. Vaggi, et al.; PLoS Comput. Biol. 7, e1002088 (2011)