Recombinant Mouse Vitronectin (VTN) Protein (His&Myc)

Name: Recombinant Mouse Vitronectin (VTN) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00643P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins, Recombinant proteins fall special offers - full-length proteins, Recombinant vitronectin (vtn) proteins

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Product Overview

Description	Recombinant Mouse Vitronectin (VTN) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P29788
Target Symbol	VTN
Synonyms	(VN)(S-protein)(Serum-spreading factor)
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DQESCKGRCTQGFMASKKCQCDELCTYYQSCCADYMEQCKPQVTRGDVFTMPEDDYWSYDYVEEPKNNTNTGVQPENTSPPGDLNPRTDGTLKPTAFLDPEEQPSTPAPKVEQQEEILRPDTTDQGTPEFPEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPGYPRNISEGFSGIPDNVDAAFALPAHRYSGRERVYFFKGKQYWEYEFQQQPSQEECEGSSLSAVFEHFALLQRDSWENIFELLFWGRSSDGAREPQFISRNWHGVPGKVDAAMAGRIYVTGSLSHSAQAKKQKSKRRSRKRYRSRRGRGHRRSQSSNSRRSSRSIWFSLFSSEESGLGTYNNYDYDMDWLVPATCEPIQSVYFFSGDKYYRVNLRTRRVDSVNPPYPRSIAQYWLGCPTSEK
Expression Range	20-478aa
Protein Length	Full Length of Mature Protein
Mol. Weight	60.2 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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.
Subcellular Location	Secreted, extracellular space.
Database References	KEGG: mmu:22370 STRING: 10090.ENSMUSP00000017488 UniGene: Mm.3667
Tissue Specificity	Plasma.

Gene Functions References

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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.