BD Transduction Laboratories™ Purified Mouse Anti-VASP
Clone 43/VASP (RUO)
Western blot analysis of VASP on human endothelial cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-VASP.
Immunoflurorescent staining on Human Endothelial cells.
Western blot analysis of VASP on human endothelial cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-VASP.
Immunoflurorescent staining on Human Endothelial cells.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Vasodilator-stimulated phosphoprotein (VASP), a substrate for cAMP- and cGMP-dependent kinases, is associated with actin filaments, focal adhesions, and dynamic membrane regions. VASP is composed of several distinct domains: a central L-proline-rich domain contains a GPPPPP motif as a single copy and as a three-fold tandem repeat, as well as three conserved phosphorylation sites for cyclic nucleotide-dependent protein kinases (Ser157, Ser239, and Thr278). A C-terminal domain contains a repetitive mixed-charge cluster which is predicted to form an α-helix. The C-terminal domain appears to be responsible for anchoring at focal adhesion sites. VASP has been shown to be a ligand for profilins. Profilins bind to the poly-L-proline motifs of VASP and it is postulated that these two molecules act in concert to convey signal transduction to actin filament formation.
Development References (5)
-
DeMali KA, Barlow CA, Burridge K. Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J Cell Biol. 2002; 159(5):881-891. (Clone-specific: Western blot). View Reference
-
Haffner C, Jarchau T, Reinhard M, Hoppe J, Lohmann SM, Walter U. Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. EMBO J. 1995; 14(1):19-27. (Biology). View Reference
-
Howe AK, Hogan BP, Juliano RL. Regulation of vasodilator-stimulated phosphoprotein phosphorylation and interaction with Abl by protein kinase A and cell adhesion. J Biol Chem. 2002; 277(41):38121-38126. (Clone-specific: Western blot). View Reference
-
Lawrence DW, Pryzwansky KB. The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading. J Immunol. 2001; 166(9):5550-5556. (Clone-specific: Immunofluorescence, Immunoprecipitation, Western blot). View Reference
-
Reinhard M, Giehl K, Abel K. The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 1995; 14(8):1583-1589. (Biology). View Reference
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.