Vitronectin (VTN) (NM_000638) Human Recombinant Protein

CAT#: TP750077

Purified recombinant protein of Human vitronectin (VTN), esidues 62-478aa, Tag free, expressed in E.coli, 50ug

Product Images

Specifications

Product Data

• Species: Human
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  A DNA sequence encoding the region (Vla62-Leu478) of VTN
• Tag: Tag Free
• Predicted MW: 47.5 kDa
• Concentration: >0.05 µg/µL as determined by Bradford protein assay method.
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: PBS, pH 7.4, 8% trehalose
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.

Reference Data

• RefSeq: NP_000629
• Locus ID: 7448
• UniProt ID: P04004, D9ZGG2
• Cytogenetics: 17q11.2
• Refseq Size: 1678
• Refseq ORF: 1434
• 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]
• Protein Families: Druggable Genome, Secreted Protein
• Protein Pathways: ECM-receptor interaction, Focal adhesion