Fibronectin Recombinant Protein | FN1 recombinant protein

Recombinant Human Fibronectin

Cat. Num. AAA968146

• Gene Names: FN1; FN; CIG; FNZ; MSF; ED-B; FINC; GFND; LETS; GFND2
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Fibronectin; Recombinant Human Fibronectin; Cold-insoluble globulin; CIG; FN1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 732-903
• Sequence: TASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPR
• Sequence Length: 2446

• Product Note: Applications are user defined. Product is developed and quality control tested in house, data or additional information may be provided upon request. The researcher needs to establish and confirm the suitability of the product for their application.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

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Related Product Information for FN1 recombinant protein

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. 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.

Product Categories/Family for FN1 recombinant protein

Immunology; Raw Materials Assay Development

References

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Proteomics 96:253-262(2014) 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin.Baron M., Main A.L., Driscoll P.C., Mardon H.J., Boyd J., Campbell I.D.Biochemistry 31:2068-2073(1992) The three-dimensional structure of the tenth type III module of fibronectin an insight into RGD-mediated interactions.Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D.Cell 71:671-678(1992) Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity.Williams M.J., Phan I., Harvey T.S., Rostagno A., Gold L.I., Campbell I.D.J. Mol. Biol. 235:1302-1311(1994) High-resolution structural studies of the factor XIIIa crosslinking site and the first type 1 module of fibronectin.Potts J.R., Phan I., Williams M.J., Campbell I.D.Nat. Struct. Biol. 2:946-950(1995) Solution structure of the glycosylated second type 2 module of fibronectin.Sticht H., Pickford A.R., Potts J.R., Campbell I.D.J. Mol. 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U.S.A. 105:12254-12258(2008) Solution structure of the 11th FN1 domain from human fibronectin 1.RIKEN structural genomics initiative (RSGI) Submitted (MAR-2008) to the PDB data bankIdentification and structural analysis of type I collagen sites in complex with fibronectin fragments.Erat M.C., Slatter D.A., Lowe E.D., Millard C.J., Farndale R.W., Campbell I.D., Vakonakis I.Proc. Natl. Acad. Sci. U.S.A. 106:4195-4200(2009) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) Mutations in FN1 cause glomerulopathy with fibronectin deposits.Castelletti F., Donadelli R., Banterla F., Hildebrandt F., Zipfel P.F., Bresin E., Otto E., Skerka C., Renieri A., Todeschini M., Caprioli J., Caruso R.M., Artuso R., Remuzzi G., Noris M.Proc. Natl. Acad. Sci. U.S.A. 105:2538-2543(2008) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 807066342
• NCBI GeneID: 2335
• NCBI Accession #: NP_001293058.1
• NCBI GenBank Nucleotide #: NM_001306129.1
• UniProt Accession #: P02751; O95609; O95610; Q14312; Q14325; Q14326; Q17RV7; Q564H7; Q585T2; B7ZLF0; E9PE77; E9PG29
• Molecular Weight: 22.8kD
• NCBI Official Full Name: fibronectin isoform 8
• 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
• 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. The encoded preproprotein is proteolytically processed to generate the mature protein. 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, at least one of which encodes an isoform that undergoes proteolytic processing. The full-length nature of some variants has not been determined. [provided by RefSeq, Jan 2016]

Uniprot Description

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.