Recombinant Human Vitronectin/VTN Protein (His Tag)(Active) | PKSH033218

Recombinant Human Vitronectin/VTN Protein (His Tag)(Active) | PKSH033218 | Gentaur US, UK & Europe Disrtribition

Synonyms: Vitronectin; VN; S-Protein; Serum-Spreading Factor; V75; VTN

Active Protein: Active protein

Activity: Recombinant Human Vitronectin is produced by our Mammalian expression system and the target gene encoding Asp20-Leu478 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Human Vitronectin is produced by our Mammalian expression system and the target gene encoding Asp20-Leu478 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-6His

Species: Human

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 53.4 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl, pH 8.0.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Human Vitronectin/VTN is a cell adhesion and spreading factor. It can be found in the blood and the extracellular matrix (ECM). Vitronectin interacts with glycosaminoglycans and proteoglycans. The multimeric Vitronectin can efficiently bind to and incorporate into the ECM; Vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Vitronectin can be recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecular. It can as a inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Vitronectin contains an endogenous cleavage site; plus cleavage sites for elastase; thrombin; and plasmin.

Research Area: Cardiovascular, immunology