Recombinant Mouse Vitronectin (Vtn)

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Vtn

Uniprot NO.

P29788

Species

Mus musculus (Mouse)

Source

Yeast

Expression Region

20-478

Target Protein Sequence

D QESCKGRCTQ GFMASKKCQC DELCTYYQSC CADYMEQCKP QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP GDLNPRTDGT LKPTAFLDPE EQPSTPAPKV EQQEEILRPD TTDQGTPEFP EEELCSGKPF DAFTDLKNGS LFAFRGQYCY ELDETAVRPG YPKLIQDVWG IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR NISEGFSGIP DNVDAAFALP AHRYSGRERV YFFKGKQYWE YEFQQQPSQE ECEGSSLSAV FEHFALLQRD SWENIFELLF WGRSSDGARE PQFISRNWHG VPGKVDAAMA GRIYVTGSLS HSAQAKKQKS KRRSRKRYRS RRGRGHRRSQ SSNSRRSSRS IWFSLFSSEE SGLGTYNNYD YDMDWLVPAT CEPIQSVYFF SGDKYYRVNL RTRRVDSVNP PYPRSIAQYW LGCPTSEK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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.

Gene References into Functions

The effects of genetic alterations in PAI-1 expression, pharmacologic PAI-1 inhibition and recombinant PAI-1 on smooth muscle cell vitronectin (VN) expression were studied, and vascular VN expression in wild-type and PAI-1-deficient mice was assessed. PMID:29028290
this study demonstrates in a mouse infection model that Vn reduces complement-mediated killing of Yersinia enterocolitica O:9 E40 and, thus, improves bacterial survival PMID:27798934
the TGF-beta-PAI-1-vitronectin-integrin axis may represent a critical convergence of factors in determining the alveolar epithelial cell apoptotic response during lung injury. PMID:27106291
In vtn knockout mice, neuronal differentiation in the cerebellum was suppressed compared with wild-type mice. PMID:26640242
PAI-1, through its interaction with Vn, exerts multiple deleterious mechanisms to induce AKI. PMID:25799354
These data suggest that adhesion to vitronectin allows for the uncoupling of fibronectin fibril formation from downstream signaling events by reducing alpha5beta1 integrin activation and fibronectin fibril extension. PMID:24509439
Report role of vitronectin in the regulation of angiogenesis induced by VEGF. PMID:24603119
Vitronectin inhibits efferocytosis through interactions with apoptotic cells as well as with macrophages. PMID:23345331
VN plays a previously unrecognized role in regulating endothelial permeability via conformational- and integrin-dependent effects on VE-cadherin trafficking. PMID:22606350
ability of vitronectin to enhance neutrophil viability was dependent on activation of phosphatidylinositol 3-kinase and extracellular signal-regulated kinase 1/2 kinases, but not on the p38 kinase PMID:22281987
These results demonstrate that vitronectin exerts a deleterious role independently from complement, by directing PAI-dependent fibrinolysis in the glomerular compartment. PMID:21764994
the vitronectin-binding capacity of PAI-1 was the primary determinant required for its ability to exacerbate lung scarring induced by intratracheal bleomycin administration PMID:21734232
Suggest that despite significant interstitial Vtn deposition in the ureteral obstruction model of chronic kidney disease, its fibrogenic role is either nonessential or redundant. PMID:21270094
Plasminogen activator inhibitor-1 and vitronectin expression level and stoichiometry regulate vascular smooth muscle cell migration through physiological collagen matrices PMID:20492459
Endogenous vitronectin promotes neointima formation in carotid arteries. PMID:12067901
regulation of cell spreading on vitronectin by ERK1 association with alphaVbeta3 integrin PMID:12393886
In a carotid artery ligation model, vitronectin (VN) knockout mice generate a larger intima than wild-type as a result of more extensive smooth muscle cell (SMC)proliferation, demonstrating that VN inhibits thrombin-mediated SMC proliferation. PMID:12482822
vitronectin can selectively regulate inactivating potassium current in embryonic hippocampal neurons PMID:12562917
competition with plasminogen activator inhibitor type-1 for alphavbeta3 binding inhibits insulin signaling PMID:12603314
in contrast to released platelet granule Vn which enhances platelet aggregation, plasma Vn inhibits platelet aggregation PMID:15733060
There is an increase of vitronectin and integrin alphav in the retina and the optic nerve after optic nerve injury. Induction of Vitronectin and integrin alphav may have an important role in the regeneration of adult mammalian retinal ganglion cells. PMID:16479252
PrP(C) plays an important role in axonal growth, and this function may be rescued in PrP(C)-knockout animals by integrin compensatory mechanisms. PMID:17504807
a novel vitronectin-dependent mechanism contributing to the development of acute lung injury. PMID:17982099
VN is a key determinant of the antiproliferative effect of PAI-1 overexpression. PMID:19574558