Recombinant Human VASP protein
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(2 Publications)
Recombinant Human VASP protein is a Human Fragment protein, in the 1 to 343 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
Vasodilator-stimulated phosphoprotein, VASP
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human VASP protein (AB105601)
15% SDS-PAGE showing ab105601 (3 μg) at approximately 37.5 kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
VASP is an important component in cell movement regulation. It acts within a larger complex of actin-binding proteins that control the assembly of actin filaments. This protein influences cell adhesion migration and signal transduction processes. Through these actions VASP influences cellular responses to environmental cues making it essential for cellular dynamics and integrity during development and wound healing.
Pathways
VASP connects to significant signaling pathways such as the PI3K/Akt pathway and the cAMP pathway. It often interacts with proteins like c-Abl tyrosine kinase and Mena contributing to actin dynamics regulation. These pathways are critical for transducing signals from extracellular environments to intracellular responses allowing for coordinated cellular functions in processes such as cell migration and growth.
Specifications
Form
Liquid
Additional notes
ab105601 is purified using conventional chromatography techniques.
General info
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.
Sequence similarities
Belongs to the Ena/VASP family.
Post-translational modifications
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.
Subcellular localisation
Cytoskeleton
Target data
Publications (2)
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Heliyon 10:e37110 PubMed39296110
2024
Applications
Unspecified application
Species
Unspecified reactive species
Communications biology 5:795 PubMed35941177
2022
Applications
Unspecified application
Species
Unspecified reactive species
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