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Human Fibronectin (32-602) Protein 2658

$300.00$1,000.00

Summary

  • Expression: HEK293
  • Pure: Yes (HPLC)
  • Amino Acid Range: Gln32-Leu602
SKU: 2658parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

P02751

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Fibronectin is a high molecular glycoprotein present in the blood, connective tissue and at cell surface. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding extracellular matrix. Fibronectin has affinity to the other main components of extracellular matrix, collagen and glycosaminoglycans.

molecular weight

The protein has a predicted MW of 65.47 kDa. Due to glycosylation, the protein migrates to 70-80 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human Fibronectin (32-602) Protein 2658

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Fibronectin is a high molecular glycoprotein present in the blood, connective tissue and at cell surface. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding extracellular matrix. Fibronectin has affinity to the other main components of extracellular matrix, collagen and glycosaminoglycans.
Protein names
Fibronectin (FN) (Cold-insoluble globulin) (CIG) [Cleaved into: Anastellin; Ugl-Y1; Ugl-Y2; Ugl-Y3]
Gene names
FN1,FN1 FN
Mass
272320Da
Function
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3900070, PubMed:3593230, PubMed:7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3900070, PubMed:3593230, 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.
Subellular location
Secreted, extracellular space, extracellular matrix. Secreted .
Tissues
Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959). 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 (PubMed:17614963).
Structure
Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP (PubMed:12225811). Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain); this interaction enhances fibronectin fibril assembly. TNFAIP6 may act as a bridging molecule between FN1 and THBS1 (PubMed:18042364). Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3 and MYOC. Interacts with SVEP1 (By similarity).; (Microbial infection) Interacts with S.aureus FnbA.; (Microbial infection) Interacts with M.bovis FbpB via the collagen-binding region.; (Microbial infection) Interacts with recombinant S.pneumoniae PavA (rqcH).; (Microbial infection) Interacts with recombinant S.suis FbpS (rqcH) via fibronectin's N-terminal 30 kDa region.; (Microbial infection) Interacts with fibronectin-binding proteins from other Mycobacteria.
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.; Serotonylated on Gln residues by TGM2 in response to hypoxia.
Target Relevance information above includes information from UniProt accession: P02751
The UniProt Consortium

HPLC of Human Fibronectin (32-602) Protein
The purity of Human Fibronectin (32-602) is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human Fibronectin (32-602) Protein
Human Fibronectin (32-602) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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We haven't added any publications to our database yet.
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

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