VASP Human
Vasodilator-stimulated phosphoprotein, VASP.
Description
VASP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 363 amino acids (1-343 a.a.) and having a molecular mass of 37.5kDa (Molecular weight on SDS-PAGE will appear higher).
The VASP is purified by proprietary chromatographic techniques.
Product Specs
Vasodilator-stimulated phosphoprotein, VASP.
MGSSHHHHHH SSGLVPRGSH MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSD.
Product Science Overview
Vasodilator-Stimulated Phosphoprotein (VASP) is a member of the Ena-VASP protein family, which plays a crucial role in actin dynamics and cell motility. VASP is a major substrate for cyclic nucleotide-dependent kinases in platelets and other cardiovascular cells . It is involved in the inhibition of agonist-induced platelet aggregation by cyclic nucleotides and the adhesion of platelets to the vascular wall .
VASP contains an N-terminal EVH1 domain that binds proteins containing E/DFPPPPXD/E motifs, targeting Ena-VASP proteins to focal adhesions and cell membranes . The protein also has a proline-rich central region and a C-terminal EVH2 domain, which is responsible for binding to actin and promoting actin nucleation .
VASP is involved in various cellular processes, including:
- Actin Dynamics: VASP promotes actin nucleation and binds to actin filaments, playing a critical role in the remodeling of the cytoskeletal architecture in response to external stimuli .
- Cell Motility: VASP is essential for directional locomotion, which requires locally confined membrane protrusion driven by actin polymerization .
- Platelet Aggregation: VASP inhibits agonist-induced platelet aggregation by cyclic nucleotides, contributing to the regulation of platelet function and thrombus formation .
Phosphorylation of VASP by cyclic nucleotide-dependent kinases, such as cAMP-dependent kinase, regulates its interaction with actin. Phosphorylation negatively affects both actin nucleation and VASP’s interaction with actin filaments . This regulation is crucial for controlling actin dynamics and cell motility.
VASP interacts with various proteins, including profilin, vinculin, and zyxin, which are involved in the formation of focal adhesions and stress fibers . Additionally, VASP forms a complex with the Crk-like protein (Crkl), which plays a role in the regulation of Rap1b, a key player in integrin signaling .
Understanding the function and regulation of VASP is essential for developing therapeutic strategies for cardiovascular diseases and disorders related to platelet function. Recombinant human VASP is used in research to study its role in cellular processes and its potential as a therapeutic target.
