Product Details
Alternative Name: | Vasodilator stimulated phosphoprotein |
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Host: | Rabbit |
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Immunogen: | Recombinant human VASP (vasodilator stimulated phosphoprotein) fused to a His-tag. |
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UniProt ID: | P50552 |
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Species reactivity: | Human
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Specificity: | Recognizes unphosphorylated as well as phosphorylated (Ser157) VASP. |
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Crossreactivity: | Does not cross-react with mouse or rat VASP. For the detection of mouse VASP use Prod. No. ALX-210-880. |
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Applications: | IF, WB
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Recommended Dilutions/Conditions: | Immunofluorescence of formaldehyde fixed cells (1:500-1:1000) Western Blot (1:1500-1:3000) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
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Formulation: | Liquid. Contains 0.02% sodium azide. |
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Handling: | Avoid freeze/thaw cycles. |
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Shipping: | Blue Ice |
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Short Term Storage: | +4°C |
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Long Term Storage: | -20°C |
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Scientific Background: | VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization: a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif b) a more divergent proline-rich central domain (which is responsible for profilin binding) c) a conserved C-terminal EVH2 domain.
VASP is expressed in a variety of mammalian cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens. |
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Regulatory Status: | RUO - Research Use Only |
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Figure: Western blot comparing three different PAbs to VASP using 25µg human platelet protein. Lane 1: PAb to VASP (human) (Prod. N. ALX-210-898). Lane 2: PAb to VASP (M4) (Prod. N. ALX-210-725) (Not available anymore!). Lane 3: PAb to VASP (affinity purified) (Prod. N. ALX-210-880).
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Product Literature References
Cyclic nucleotide phosphodiesterase 1 regulates lysosome-dependent type I collagen protein degradation in vascular smooth muscle cells: Y. Cay, et al.; Arterioscler. Thromb. Vasc. Biol.
31, 616 (2011),
Abstract;
Full Text
Proteomics identifies thymidine phosphorylase as a key regulator of the angiogenic potential of colony-forming units and endothelial progenitor cell cultures: G. Pula, et al.; Circ. Res.
104, 32 (2009),
Abstract;
Full Text
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