Recombinant Human Fibronectin Protein

重组人Fibronectin蛋白 | 重组人纤连蛋白

CIG | ED-B | fibronectin 1 | Fibronectin | FINC | FN | FN1 | FNZ | GFND | GFND2 | LETS | MSF | SMDCF | Cold insoluble globulin | Cold-insoluble globulin | DKFZp686F10164 | DKFZp686H0342 | DKFZp686I1370 | DKFZp686O13149 | ED B | FINC_HUMAN | Migration stim

rp176702-10μg

10μg

无动物源

≥90%(SDS-PAGE)

Fibronectin (FN) is a large, modular glycoprotein that generates a polymeric fibrillar network in the extracellular matrix (ECM), and forms soluble, disulfide-linked dimeric protomers in plasma and other body fluids. Fibronectin is a ligand for many molecules, including fibrin, heparin, chondroitin sulfate, collagen/gelatin, and integrins. It is involved in multiple cellular processes such as cell adhesion/migration, blood clotting, morphogenesis, tissue repair, and cell signaling. Fibronectin functions are mediated by the insoluble polymeric fibrillar network. Conversion of soluble Fibronectin to Fibronectin fibrils in the ECM is initiated by binding to cell surface integrins, resulting in exposure of cryptic epitopes necessary for polymerization. Fibronectin is made up of three types of homologous structural motifs termed FN type I, type II, and type III repeats. Alternative splicing generates multiple isoforms of Fibronectin which may have insertions of extra type III domains (EDA and EDB) or alteration of the type III connecting segment (IIICS). Differential splicing within the IIICS domain determines the presence of CS1 and CS2 sequences, and its sensitivity to proteases. The tilt angle between type III domains #9 and #10 (which contains an RGD motif) determines integrin binding affinity, suggesting how structural differences between fibrillar and soluble Fibronectin may influence their function. From the N-terminus to the furin cleavage site at amino acid 1908, human Fibronectin shares 92% amino acid sequence identity with mouse and rat Fibronectin. Post-translational: Sulfated.It is not known whether both or only one of Thr-2155 and Thr-2156 are/is glycosylated.Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).Phosphorylated by FAM20C in the extracellular medium.Proteolytic processing produces the C-terminal NC1 peptide, anastellin.Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.Serotonylated on Gln residues by TGM2 in response to hypoxia.

Measured by the ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells.

重组表达

24.0 kDa

C-His

27.7-32.3 kDa, under reducing conditions

HEK293 Accession #: P02751 | HEK293

<1.0 EU/μg

人(Human)

2177-2386 aa

MEAPAQLLFLLLLWLPDTTGIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCHHHHHH

Yes

Yes