Species : |
Human |
Source : |
Mammalian Cells |
Tag : |
Flag |
Description : |
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. |
Form : |
25 mM Tris HCl, pH 7.3, 100 mM glycine, 10% glycerol. |
Molecular Mass : |
39.6 kDa |
AA Sequence : |
MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGV KYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVEQ QKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPPL PAAQGPGGGGAGAPGLAAAIAGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQV GEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQE LLEEVKKELQKVKEEIIEAFVQELRKRGSPTRTRPLEQKLISEEDLAANDILDYKDDDDKV |
Purity : |
> 80% as determined by SDS-PAGE and Coomassie blue staining. |
Stability : |
Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : |
Store at -80 centigrade. |
Concentration : |
>50 ug/mL as determined by microplate BCA method. |
Preparation : |
Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps. |
Protein Families : |
Druggable Genome, Stem cell - Pluripotency |
Protein Pathways : |
Fc gamma R-mediated phagocytosis, Focal adhesion, Leukocyte transendothelial migration |
Full Length : |
Full L. |