protein

Human Vitronectin

MBS691940

0.5 mg

340 USD

Recombinant Protein

Human Vitronectin

Vitronectin

Recombinant Human Vitronectin

vitronectin; Vitronectin; vitronectin; epibolin; S-protein; somatomedin B; complement S-protein; serum spreading factor; serum-spreading factor; vitronectin; S-protein; Serum-spreading factor; V75

VTN; VTN; VN; V75; VNT; VN

VTNC_HUMAN

HEK 293 Cells

Human

478

DQESCKGRCT EGFNVDKKCQ CDELCSYYQS CCTDYTAECK PQVTRG DVFT MPEDEYTVYD DGEEKNNATV HEQVGGPSLT SDLQAQSKGN P EQTPVLKPE EEAPAPEVGA SKPEGIDSRP ETLHPGRPQP PAEEELC SGK PFDAFTDLKN GSLFAFRGQY CYELDEKAVR PGYPKLIRDV WG IEGPIDAA FTRINCQGKT YLFKGSQYWR FEDGVLDPDY PRNISDGF DG IPDNVDAALA LPAHSYSGRE RVYFFKGKQY WEYQFQHQPS QEE CEGSSLS AVFEHFAMMQ RDSWEDIFEL LFWGRTSAGT RQPQFISRD W HGVPGQVDAA MAGRIYISGM APRPSLAKKQ RFRHRNRKGY RSQR GHSRGR NQNSRRPSRA TWLSLFSSEE SNLGANNYDD YRMDWLVPAT CEPIQSVFFF SGDKYYRVNL RTRRVDTVDP PYPRSIAQYW LGCPA PGHL

>95% by SDS-PAGE and HPLC analysis

Lyophilized

Reconstitution: Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do Not Vortex! For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20 degree C to -80 degree C. Stability: The lyophilized protein is stable at room temperature for up to 1 month and at 4 degree C for 3 months. Working aliquots stored with a carrier protein are stable for at least 3 months at -20 degree C to -80 degree C. Avoid repeated freeze-thaw cycles.

Endotoxin Level: < 0.1 ng per ug of Vitronectin

Biological Activity: Testing under progress.

Cytokines & Growth Factors

Vitronectin is a secreted glycoprotein which is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide linked multimers. The multimeric Vitronectin can efficiently bind to and incorporate into the extracellular matrix. Within the matrix, Vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically defined matrix component in human embryonic stem cell renewal media. Recombinant human Vitronectin is a 459 amino acid single chain monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions.

88853069

NP_000629.3

NM_000638.3

P04004

52.2kDa

Complement Cascade Pathway (106405); ECM Proteoglycans Pathway (833812); ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Elastic Fibre Formation Pathway (730310); Extracellular Matrix Organization Pathway (576262); FOXA1 Transcription Factor Network Pathway (137979); Focal Adhesion Pathway (198795); Focal Adhesion Pathway (83067); Focal Adhesion Pathway (478)

The protein encoded by this gene is a member of the pexin family. It is found in serum and tissues and promotes cell adhesion and spreading, inhibits the membrane-damaging effect of the terminal cytolytic complement pathway, and binds to several serpin serine protease inhibitors. It is a secreted protein and exists in either a single chain form or a clipped, two chain form held together by a disulfide bond. [provided by RefSeq, Jul 2008]

Function: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. Subunit structure: Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1, insulin and C1QBP. Ref.9 Ref.10 Ref.15 Ref.16. Subcellular location: Secreted extracellular space. Tissue specificity: Plasma. Domain: The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin. Post-translational modification: Sulfated on 2 tyrosine residues.N- and O-glycosylated . By similarity. Ref.22 Ref.25Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.Phosphorylation sites are present in the extracellular medium. Sequence similarities: Contains 4 hemopexin repeats.Contains 1 SMB (somatomedin-B) domain.

0.5 mg

340 USD