Fibronectin Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [JF0582] (HA750340)

UNIPROT #

P02751

PROTEIN NAME

Fibronectin

SYNONYMS

CIG antibody;Cold insoluble globulin antibody;Cold-insoluble globulin antibody;DKFZp686F10164 antibody;DKFZp686H0342 antibody;DKFZp686I1370 antibody;DKFZp686O13149 antibody;ED B antibody;Fibronectin 1 antibody;FINC antibody;FINC_HUMAN antibody;FN antibody;FN1 antibody;FNZ antibody;GFND antibody;GFND2 antibody;LETS antibody;Migration stimulating factor antibody;MSF antibody;Ugl-Y3 antibody

TISSUE SPECIFICITY

Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level). Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine.

DEVELOPMENTAL STAGE

Expressed between 12 and 19 weeks post-conception (WPC) in Bruch's membrane, with expression in the choroid evident from 14 WPC onwards (at protein level). Expressed in the inner limiting membrane at 17 WPC (at protein level). Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age.

POST-TRANSLATIONAL MODIFICATION

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.

SUBCELLULAR LOCATION

Secreted, extracellular space, extracellular matrix.

FUNCTION

Fibronectin is an extracellular matrix glycoprotein present on most cell surfaces, in extracellular fluids and in plasma. A high molecular weight heterodimeric protein, it was originally discovered as a protein missing from the surfaces of virus-transformed cells, and it has been shown to be involved in various functions including cell adhesion, cell motility and wound healing. Alternative splicing and glycosylation give rise to several different forms of Fibronectin, some of which exhibit restricted tissue distribution or association with malignancies. It has been shown that Myofibroblast phenotype formation correlates with the occurrence of glycosylated Fibronectin and Fibronectin splice variants in Dupuytren's disease.