Fibronectin Fragment Peptide | FN1 peptide

Fibronectin Fragment (Gly-Arg-Ala-Asp-Ser-Pro-Lys) (GRADSPK)

Cat. Num. AAA658374

• Gene Names: FN1; FN; CIG; FNZ; MSF; ED-B; FINC; GFND; LETS; GFND2
• Purity: Highly Purified; ~95%. Purified by HPLC.
• Synonyms: Fibronectin Fragment; Fibronectin Fragment (Gly-Arg-Ala-Asp-Ser-Pro-Lys) (GRADSPK); FN1 peptide

• Host: Synthetic peptide
• Purity/Purification: Highly Purified; ~95%. Purified by HPLC.
• Form/Format: Supplied as a lyophilized powder.

• Sequence (linear): Gly-Arg-Ala-Asp-Ser-Pro-Lys (GRADSPK)
• Preparation and Storage: Lyophilized powder may be stored at 4 degree C for short-term only. Stable for 12 months at -20 degree C. Reconstitute to nominal volume (see reconstitution instructions for peptides) and store at -20 degree C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.

Product Categories/Family for FN1 peptide

Molecular Biology; MB-Peptides

NCBI and Uniprot Product Information

• NCBI GI #: 300669710
• NCBI GeneID: 2335
• UniProt Accession #: P02751; O95609; O95610; Q14312; Q14325; Q14326; Q17RV7; Q564H7; Q585T2; B7ZLF0; E9PE77; E9PG29
• Molecular Weight: 262,625 Da
• NCBI Official Full Name: Fibronectin
• NCBI Official Synonym Full Names: fibronectin 1
• NCBI Official Symbol: FN1
• NCBI Official Synonym Symbols: FN; CIG; FNZ; MSF; ED-B; FINC; GFND; LETS; GFND2
• NCBI Protein Information: fibronectin; cold-insoluble globulin; migration-stimulating factor
• UniProt Protein Name: Fibronectin
• Protein Family: Fibronectin
• UniProt Gene Name: FN1
• UniProt Synonym Gene Names: FN; FN; CIG
• UniProt Entry Name: FINC_HUMAN

NCBI Description

This gene encodes fibronectin, a glycoprotein present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix. Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. The gene has three regions subject to alternative splicing, with the potential to produce 20 different transcript variants. However, the full-length nature of some variants has not been determined. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. Ref.38 Ref.40 Ref.44 Ref.50Anastellin 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. Ref.38 Ref.40 Ref.44 Ref.50

Subunit 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. Interacts with S.aureus fnbA. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth

By similarity. Interacts with FST3. Ref.36 Ref.38 Ref.39 Ref.41 Ref.42 Ref.47

Subcellular location: Secreted › extracellular space › extracellular matrix.

Tissue specificity: 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. Ref.16 Ref.35

Developmental stage: Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. Ref.16 Ref.35

Post-translational modification: Sulfated.It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated. Ref.16 Ref.26 Ref.35 Ref.58Forms 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).Phosphorylation sites are present in the extracellular medium.Proteolytic processing produces the C-terminal NC1 peptide, anastellin.

Involvement in disease: Glomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.72

Sequence similarities: Contains 12 fibronectin type-I domains.Contains 2 fibronectin type-II domains.Contains 16 fibronectin type-III domains.

Sequence caution: The sequence AAX76513.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAD93077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD91166.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD97964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD97965.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAH18136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.