VASP (NM_003370) Human 3' UTR Clone

Specifications

Product Data
Product Name	VASP (NM_003370) Human 3' UTR Clone
Vector	pMirTarget
ACCN	NM_003370
Insert Size	836 bp
Sequence Data	Insert Sequence (showhide) >SC210104 3’UTR clone of NM_003370 The sequence shown below is from the reference sequence of NM_003370. The complete sequence of this clone may contain minor differences, such as SNPs. Blue=Stop Codon Red=Cloning site GGCAAGTTGGACGCCCGCAAGATCCGCGAGATTCTCATTAAGGCCAAGAAGGGCGGAAAGATCGCCGTG TAACAATTGGCAGAGCTCAGAATTCAAGCGATCGCC CAGGAGCTGAGGAAGCGGGGTTCTCCCTGACCACAGGGACCCAGAAGACCCGCTTCTCCTTTCCGCACA CCCGGCCTGTCACCCTGCTTTCCCTGCCTCTACTTGACTTGGAATTGGCTGAAGACTACACAGGAATGC ATCGTTCCCACTCCCCATCCCACTTGGAAAACTCCAAGGGGGTGTGGCTTCCCTGCTCACACCCACACT GGCTGCTGATTGGCTGGGGAGGCCCCCGCCCTTTTCTCCCTTTGGTCCTTCCCCTCTGCCATCCCCTTG GGGCCGGTCCCTCTGCTGGGGATGCACCAATGAACCCCACAGGAAGGGGGAAGGAAGGAGGGAATTTCA CATTCCCTTGTTCTAGATTCACTTTAACGCTTAATGCCTTCAAAGTTTTGGTTTTTTTAAGAAAAAAAA ATATATATATATTTGGGTTTTGGGGGAAAAGGGAAATTTTTTTTTCTCTTTGGTTTTGATAAAATGGGA TGTGGGAGTTTTTAAATGCTATAGCCCTGGGCTTGCCCCATTTGGGGCAGCTATTTAAGGGGAGGGGAT GTCTCACCGGGCTGGGGGTGAGATATCCCCCCACCCCAGGGACTCCCCTTCCCTCTGGCTCCTTCCCCT TTTCTATGAGGAAATAAGATGCTGTAACTTTTTGGAACCTCAGTTTTTTGATTTTTTATTTGGGTAGGT TTTGGGGTCCAGGCCATTTTTTTTACCCCTTGGAGGAAATAAGATGAGGGAGAAAGGAGAAGGGGAGGA AACTTCTCCCCTCCCACCTTCACCTTTAGCTTCTTGAAAATGGGCCCCTGCAGAATAAATCTGCCAGTT TTTATAAA ACGCGTAAGCGGCCGCGGCATCTAGATTCGAAGAAAATGACCGACCAAGCGACGCCCAACCTGCCATCA CGAGATTTCGATTCCACCGCCGCCTTCTATGAAAGG
Restriction Sites	SgfI-MluI
OTI Disclaimer	Our molecular clone sequence data has been matched to the sequence identifier above as a point of reference. Note that the complete sequence of this clone is largely the same as the reference sequence but may contain minor differences , e.g., single nucleotide polymorphisms (SNPs).
Reference Data
RefSeq	NM_003370.4
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]
Locus ID	7408
MW	31.1

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