VTN Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P04004 |
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Clone Names | 80924274 |
Gene ID | 7448 |
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Other Names | Vitronectin, VN, S-protein, Serum-spreading factor, V75, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B, VTN |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7462a was selected from the N-term region of human VTN. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | VTN |
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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. |
Cellular Location | Secreted, extracellular space |
Tissue Location | Expressed in the retina pigment epithelium (at protein level) (PubMed:25136834). Expressed in plasma (at protein level) (PubMed:2448300). Expressed in serum (at protein level) (PubMed:29567995). |
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Provided below are standard protocols that you may find useful for product applications.
Background
VTN is a member of the pexin family. This protein 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. The protein is a secreted protein and exists in either a single chain form or a clipped, two chain form held together by a disulfide bond.
References
Jenne D.E., Stanley K.K.EMBO J. 4:3153-3157(1985) Sigurdardottir O., Wiman B.Biochim. Acta 1208:104-110(1994)Seiffert D., Loskutoff D.J.J. Biol. Chem. 266:2824-2830(1991)
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