Recombinant Human Fibronectin protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human Fibronectin protein is a Human Fragment protein, in the 631 to 705 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE.
View Alternative Names
FN, FN1, Fibronectin, Cold-insoluble globulin, CIG
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Fibronectin protein (AB283422)
SDS-PAGE analysis of ab283422.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Specifications
Form
Lyophilized
General info
Function
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed : 3024962, PubMed : 3593230, PubMed : 3900070, PubMed : 7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed : 3024962, PubMed : 3593230, PubMed : 3900070, PubMed : 7989369). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated monocyte activation (PubMed : 34089617).. Anastellin. Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.. Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5 : ITGB1 integrin receptor signaling.
Post-translational modifications
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.
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com