VASP Full-Length MS Protein Standard

VASP vasodilator-stimulated phosphoprotein

VASP Full-Length MS Protein Standard (NP_003361), Labeled with [U- ¹³C₆, ¹⁵N₄]-L-Arginine and [U- ¹³C₆, ¹⁵N₂]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.

VASP

vasodilator-stimulated phosphoprotein

NM_003370

19q13.32

[U- ¹³C₆, ¹⁵N₄]-L-Arg and [U- ¹³C₆, ¹⁵N₂]-L-Lys

> 80% as determined by SDS-PAGE and Coomassie blue staining

Human HEK293 cells

40.3 kDa

RC203544

>RC203544 representing NM_003370
MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGV
KYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVEQ
QKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPPL
PAAQGPGGGGAGAPGLAAAIAGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQV
GEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQE
LLEEVKKELQKVKEEIIEAFVQELRKRGSP