VASP (NM_003370) Human Mass Spec Standard

Specifications

Product Data
Description	VASP MS Standard C13 and N15-labeled recombinant protein (NP_003361)
Species	Human
Expression Host	HEK293
Expression cDNA Clone or AA Sequence	RC203544
Predicted MW	40.3 kDa
Protein Sequence	Sequence Link (showhide) >RC203544 representing NM_003370 Red=Cloning site Green=Tags(s) MSSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRG VKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVE QQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPP LPAAQGPGGGGAGAPGLAAAIAGAKLRKVSKEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQV GEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQE LLEEVKKELQKVKEEIIEAFVQELRKRGSP TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-Myc/DDK
Purity	> 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration	>0.05 µg/µL as determined by microplate BCA method
Labeling Method	Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Buffer	25 mM Tris-HCl, 100 mM glycine, pH 7.3
Reference Data
RefSeq	NP_003361
RefSeq Size	2298
RefSeq ORF	1140
Locus ID	7408
Cytogenetics	19q13.32
Summary	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. [provided by RefSeq, Jul 2008]
Protein Families	Druggable Genome, Stem cell - Pluripotency
Protein Pathways	Fc gamma R-mediated phagocytosis, Focal adhesion, Leukocyte transendothelial migration

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