Mouse Recombinant VTN protein, His Tag (V2LY-0526-LY9071)

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Datasheet Target Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host
HEK293 Cells
Protein Species
Mouse
Tag
His Tag
Protein Construction
This product is Mouse Recombinant VTN protein, His Tag consist of Amino Acid: 1-478 and predicts a molecular mass of 54.2 kDa.
Molecule Mass
54.2 kDa
Sequence
Amino Acid: 1-478
Species
Mouse

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>85% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Vitronectin
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.
Biological Process
Biological Process cell adhesion Source:ProtInc1 Publication
Biological Process cell adhesion mediated by integrin Source:BHF-UCL1 Publication
Biological Process cell migration Source:UniProtKB1 Publication
Biological Process cell-matrix adhesion Source:BHF-UCL1 Publication
Biological Process endodermal cell differentiation Source:UniProtKB1 Publication
Biological Process extracellular matrix organization Source:Ensembl
Biological Process immune response Source:ProtInc1 Publication
Biological Process liver regeneration Source:Ensembl
Biological Process negative regulation of blood coagulation Source:BHF-UCL1 Publication
Biological Process negative regulation of endopeptidase activity Source:BHF-UCL1 Publication
Biological Process negative regulation of fibrinolysis Source:ComplexPortal1 Publication
Biological Process oligodendrocyte differentiation Source:Ensembl
Biological Process positive regulation of cell-substrate adhesion Source:Ensembl
Biological Process positive regulation of peptidyl-tyrosine phosphorylation Source:BHF-UCL1 Publication
Biological Process positive regulation of protein binding Source:BHF-UCL1 Publication
Biological Process positive regulation of receptor-mediated endocytosis Source:BHF-UCL1 Publication
Biological Process positive regulation of smooth muscle cell migration Source:BHF-UCL1 Publication
Biological Process positive regulation of vascular endothelial growth factor receptor signaling pathway Source:BHF-UCL1 Publication
Biological Process positive regulation of wound healing Source:BHF-UCL1 Publication
Biological Process protein polymerization Source:Ensembl
Biological Process regulation of cell adhesion Source:ComplexPortal1 Publication
Biological Process smooth muscle cell-matrix adhesion Source:BHF-UCL1 Publication
Cellular Location
Secreted, extracellular space
Parasitophorous vacuole
(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995).
Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995).
PTM
Sulfated on tyrosine residues.
N- and O-glycosylated.
Phosphorylation 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.
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For research use only. Not intended for any clinical use.

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