anti-Vitronectin antibody for Western blot,IHC-Formalin-fixed paraffin-embedded sections,ICC/IF and Human,Mouse,Rat
|Product Description||Rabbit Polyclonal antibody recognizes Vitronectin|
|Tested Reactivity||Hu, Ms, Rat|
|Tested Application||ICC/IF, IHC-P, WB|
|Immunogen||Synthetic peptide derived from Human Vitronectin.|
|Alternate Names||Vitronectin; V75; VN; Serum-spreading factor; S-protein; VNT|
|Application Note||* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.|
|Buffer||PBS (pH 7.4), 150 mM NaCl, 0.02% Sodium azide and 50% Glycerol.|
|Preservative||0.02% Sodium azide|
|Storage instruction||For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.|
|Note||For laboratory research only, not for drug, diagnostic or other use.|
|Gene Full Name||vitronectin|
|Background||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. [UniProt]
|Cellular Localization||Secreted, extracellular space. [UniProt]|
|Calculated MW||54 kDa|
|PTM||Sulfated on 2 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. [UniProt]
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