Vitronectin (VTN) (NM_000638) Human Recombinant Protein

CAT#: TP720655L

Purified recombinant protein of Human vitronectin (VTN)

Specifications

Product Data

• Species: Human
• Expression Host: HEK293
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  Asp20-Leu478
• Tag: C-His
• Predicted MW: 53.35 kDa
• Concentration: lot specific
• Purity: >95% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: Provided lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl
• Endotoxin: Endotoxin level is < 0.1 ng/µg of protein (< 1 EU/µg)
• Reconstitution: Always centrifuge tubes before opening. Do not mix by vortex or pipetting. Dissolve the lyophilized protein in ddH2O. It is not recommended to reconstitute a concentration less than 100 µg/ml. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
• Storage: Store at -80°C.
• Stability: Stable for at least 6 months from date of receipt under proper storage and handling conditions.

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