VTN
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Official Full Name
vitronectin -
Overview
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. Vitronectin also known as VTN is a protein that in humans is encoded by the VTN gene. The protein encoded by this gene is a member of the pexin family. Vitronectin is an abundant glycoprotein found in serum and the extracellular matrix 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. Vitronectin has been speculated to be involved in hemostasis and tumor malignancy. -
Synonyms
VTN;VN;V75;VNT;vitronectin;epibolin;S-protein;somatomedin B;OTTHUMP00000163323;complement S-protein;serum spreading factor;serum-spreading factor
Recombinant Proteins
- Human
- Mouse
- Rat
- Chicken
- Bovine
- Pig
- Rabbit
- Insect Cells
- HEK293
- E.coli
- Human Cells
- Mammalian Cells
- Mouse
- Bovine Plasma
- Porcine plasma
- Rabbit Plasma
- rat plasma
- Human Plasma
- Pig Plasma
- Rat plasma
- Mouse Plasma
- His
- Non
- DDK
- Myc
- Avi
- Fc
Involved Pathway
VTN involved in several pathways and played different roles in them. We selected most pathways VTN participated on our site, such as PIK-Akt signaling pathway,Focal adhesion,ECM-receptor interaction, which may be useful for your reference. Also, other proteins which involved in the same pathway with VTN were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Proteoglycans in cancer | EZR,Fzd4,FZD9,HCLS1,PPP1R12B,CAMK2A,TGFB2,WNT4,NRAS,HOXD10 |
| PIK-Akt signaling pathway | NFKB1,COL6A5,FGFR3,FGF21,IFNA7,THBS4,PPP2R2C,IFNA2,IGF1,PIK3R5 |
| Focal adhesion | ITGA6,PXNA,MAPK3,FYNA,TNK2,CAV2,RAC1,MYL12A,BADB,ITGB1B.2 |
| ECM-receptor interaction | LAMA5,COL4A4,LAMB1A,LAMB1,ITGB3,THBS4B,ITGB1B.2,LAMA4,TNC,ITGB8 |
Protein Function
VTN has several biochemical functions, for example, extracellular matrix binding,heparin binding,integrin binding. Some of the functions are cooperated with other proteins, some of the functions could acted by VTN itself. We selected most functions VTN had, and list some proteins which have the same functions with VTN. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| scavenger receptor activity | LOXL2B,TMPRSS13B,SCARA3,TMPRSS4B,SCARF2,GM106,SCARF1,LOXL3,LOXL3B,DMBT1 |
| heparin binding | CTGF,APOB,SLIT2,AZU1,KNG1,LPA,FMOD,IMPG2,CXCL6,WISP1A |
| integrin binding | P4HB,TSPAN4,S1PR3,LYN,CYR61,ICAM1,ADAMTS13,TNN,ECM2,S1PR2 |
| extracellular matrix binding | ITGA2B,CD248,ITGAV,TGFBI,VEGFA,SPP1,BGN,SID4,GPR56,SPOCK2 |
| protein binding | PRKD2,COG4,KRTAP9-2,HTR6,FXYD6,ARMC2,IL1RAPL1,HDAC3,ZNF576,HIST1H4A |
| polysaccharide binding | SUSD2,CD209B,ENPP1,C8orf84,ENPP2,ENDOU,GM106,VTNA,MBL1,PRG4 |
Interacting Protein
VTN has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with VTN here. Most of them are supplied by our site. Hope this information will be useful for your research of VTN.
C1QBP;GOPC;SERPINE1;PASK;ganglioside_gm1;ITGAV;ITGB5;GLUD1;f_hcvh;ADH5
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References
- Lee, YS; Ryu, SW; et al. Cross-platform meta-analysis of multiple gene expression profiles identifies novel expression signatures in acquired anthracycline-resistant breast cancer. ONCOLOGY REPORTS 33:1985-1993(2015).
- Horner, SM; Wilkins, C; et al. Proteomic Analysis of Mitochondrial-Associated ER Membranes (MAM) during RNA Virus Infection Reveals Dynamic Changes in Protein and Organelle Trafficking. PLOS ONE 10:-(2015).
