Vitronectin (VTN) (NM_000638) Human 3' UTR Clone

Specifications

Product Data
Product Name	Vitronectin (VTN) (NM_000638) Human 3' UTR Clone
Vector	pMirTarget
Synonyms	V75; VN; VNT
ACCN	NM_000638
Insert Size	115 bp
Sequence Data	Insert Sequence (showhide) >SC200508 3’UTR clone of NM_000638 The sequence shown below is from the reference sequence of NM_000638. The complete sequence of this clone may contain minor differences, such as SNPs. Blue=Stop Codon Red=Cloning site GGCAAGTTGGACGCCCGCAAGATCCGCGAGATTCTCATTAAGGCCAAGAAGGGCGGAAAGATCGCCGTG TAACAATTGGCAGAGCTCAGAATTCAAGCGATCGCC CTGGGCTGCCCAGCTCCTGGCCATCTGTAGGAGTCAGAGCCCACATGGCCGGGCCCTCTGTAGCTCCCT CCTCCCATCTCCTTCCCCCAGCCCAATAAAGGTCCCTTAGCCCCGA 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_000638.4
Synonyms	V75; VN; VNT
Summary	The protein encoded by this gene functions in part as an adhesive glycoprotein. Differential expression of this protein can promote either cell adhesion or migration as it links cells to the extracellular matrix through a variety of ligands. These ligands include integrins, plasminogen activator inhibitor-1, and urokinase plasminogen activator receptor. This secreted protein can be present in the plasma as a monomer or dimer and forms a multimer in the extracellular matrix of several tissues. This protein also inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to several serpin serine protease inhibitors. This protein can also promote extracellular matrix degradation and thus plays a role in tumorigenesis. It is involved in a variety of other biological processes such as the regulation of the coagulation pathway, wound healing, and tissue remodeling. The heparin-binding domain of this protein give it anti-microbial properties. It is also a lipid binding protein that forms a principal component of high density lipoprotein. [provided by RefSeq, Aug 2020]
Locus ID	7448
MW	3.9

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