• Call +1.858.633.0165 or Fax +1.858.633.0166 or Contact Us

Fibronectin (FN1) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS955729

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… More details

$425 / 0.2 mg +1 FREE 8GB USB
Product Documentation
PDF
Sample Manual Insert View PDF
PDF
Testing Data View PDF
PDF
Certificate of Analysis (COA) View PDF
PDF
QC Report View PDF
PDF
Material Safety Data Sheet View PDF
PDF
Technical Datasheet View PDF
PDF
Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
Fibronectin (FN1), Recombinant Protein
Full Product Name
Recombinant Human Fibronectin
Product Gene Name
Product Synonym Gene Name
FN
Product Synonym Names
Cold-insoluble globulin; CIG
Sequence
TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL PGRKYIVNVY QISEDGEQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VVIQQETTGT PRSDTVPSPR
Host
E Coli
Form/Format
Liquid containing glycerol
Purity/Purification
Greater than 90% as determined by SDS-PAGE.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
23.6kD
Sequence Positions
732-911
OMIM
135600
3D Structure
ModBase 3D Structure for P02751
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.
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for FN1 recombinant protein

Phenotypic and genetic alterations in mammary stroma implications for tumour progression.Schor S.L., Schor A.M.Breast Cancer Res. 3:373-379(2001) The expression of migration stimulating factor, a potent oncofetal cytokine, is uniquely controlled by 3'-untranslated region-dependent nuclear sequestration of its precursor messenger RNA.Kay R.A., Ellis I.R., Jones S.J., Perrier S., Florence M.M., Schor A.M., Schor S.L.Cancer Res. 65:10742-10749(2005) Vector-capping a simple method for preparing a high-quality full-length cDNA library.Kato S., Ohtoko K., Ohtake H., Kimura T.DNA Res. 12:53-62(2005) Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Human fibronectin is synthesized as a pre-propolypeptide.Gutman A., Yamada K.M., Kornblihtt A.R.FEBS Lett. 207:145-148(1986) Cloning and analysis of the promotor region of the human fibronectin gene.Dean D.C., Bowlus C.L., Bourgeois S.Proc. Natl. Acad. Sci. U.S.A. 84:1876-1880(1987) Primary structure of human fibronectin differential splicing may generate at least 10 polypeptides from a single gene.Kornblihtt A.R., Umezawa K., Vibe-Pedersen K., Baralle F.E.EMBO J. 4:1755-1759(1985) Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain.Garcia-Pardo A., Pearlstein E., Frangione B.J. Biol. Chem. 258:12670-12674(1983) Godfrey H.P., Ebrahim A.A. Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli.Owens R.J., Baralle F.E.EMBO J. 5:2825-2830(1986) Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin.Calaycay J., Pande H., Lee T., Borsi L., Siri A., Shively J.E., Zardi L.J. Biol. Chem. 260:12136-12141(1985) Identification of novel fibronectin fragments detected specifically in juvenile urine.Iida R., Yasuda T., Kishi K.FEBS J. 274:3939-3947(2007) Human fibronectin cell specific alternative mRNA splicing generates polypeptide chains differing in the number of internal repeats.Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.Nucleic Acids Res. 12:5853-5868(1984) Sequence analysis and in vivo expression show that alternative splicing of ED-B and ED-A regions of the human fibronectin gene are independent events.Paolella G., Henchcliffe C., Sebastio G., Baralle F.E.Nucleic Acids Res. 16:3545-3557(1988) Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon.Zardi L., Carnemolla B., Siri A., Petersen T.E., Paolella G., Sebastio G., Baralle F.E.EMBO J. 6:2337-2342(1987) Identification of a third region of cell-specific alternative splicing in human fibronectin mRNA.Gutman A., Kornblihtt A.R.Proc. Natl. Acad. Sci. U.S.A. 84:7179-7182(1987) The cell attachment domain of fibronectin. Determination of the primary structure.Pierschbacher M.D., Ruoslahti E., Sundelin J., Lind P., Peterson P.A.J. Biol. Chem. 257:9593-9597(1982) Molecular cloning and nucleotide sequence of a cDNA clone coding for the cell attachment domain in human fibronectin.Oldberg A., Linney E., Ruoslahti E.J. Biol. Chem. 258:10193-10196(1983) Evolution of the fibronectin gene. Exon structure of cell attachment domain.Oldberg A., Ruoslahti E.J. Biol. Chem. 261:2113-2116(1986) Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity.Garcia-Pardo A., Rostagno A., Frangione B.Biochem. J. 241:923-928(1987) Human cellular fibronectin comparison of the carboxyl-terminal portion with rat identifies primary structural domains separated by hypervariable regions.Bernard M.P., Kolbe M., Weil D., Chu M.-L.Biochemistry 24:2698-2704(1985) Human plasma fibronectin. Demonstration of structural differences between the A- and B-chains in the III CS region.Tressel T., McCarthy J.B., Calaycay J., Lee T.D., Legesse K., Shively J.E., Pande H.Biochem. J. 274:731-738(1991) Human fibronectin molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain.Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.EMBO J. 3:221-226(1984) Human liver fibronectin complementary DNAs identification of two different messenger RNAs possibly encoding the alpha and beta subunits of plasma fibronectin.Sekiguchi K., Klos A.M., Kurachi K., Yoshitake S., Hakomori S.Biochemistry 25:4936-4941(1986) Novel cartilage-specific splice variants of fibronectin.Parker A.E., Boutell J., Carr A., Maciewicz R.A.Osteoarthritis Cartilage 10:528-534(2002) Isolation and characterization of cDNA clones for human liver fibronectin.Umezawa K., Kornblihtt A.R., Baralle F.E.FEBS Lett. 186:31-34(1985) Donor and acceptor splice signals within an exon of the human fibronectin gene a new type of differential splicing.Vibe-Pedersen K., Magnusson S., Baralle F.E.FEBS Lett. 207:287-291(1986) Primary structure of human plasma fibronectin. Characterization of a 31,000-dalton fragment from the COOH-terminal region containing a free sulfhydryl group and a fibrin-binding site.Garcia-Pardo A., Pearlstein E., Frangione B.J. Biol. Chem. 260:10320-10325(1985) Isolation and characterization of cDNA clones for human and bovine fibronectins.Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.Proc. Natl. Acad. Sci. U.S.A. 80:3218-3222(1983) Tyrosine sulfation of proteins from the human hepatoma cell line HepG2.Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985) Purification of a young age-related glycoprotein (Ugl-Y) from normal human urine.Iida R., Yasuda T., Kishi K.J. Biochem. 101:357-363(1987) Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin.Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K., Argraves W.S.J. Biol. Chem. 267:20120-20125(1992) Further characterization of the NH2-terminal fibrin-binding site on fibronectin.Rostagno A., Williams M.J., Baron M., Campbell I.D., Gold L.I.J. Biol. Chem. 269:31938-31945(1994) Superfibronectin is a functionally distinct form of fibronectin.Morla A., Zhang Z., Ruoslahti E.Nature 367:193-196(1994) Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin.Sasaki T., Brakebusch C., Engel J., Timpl R.EMBO J. 17:1606-1613(1998) A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis.Yi M., Ruoslahti E.Proc. Natl. Acad. Sci. U.S.A. 98:620-624(2001) The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin.Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R., Pihlajaniemi T.J. Biol. Chem. 277:23092-23099(2002) Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin.Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P., Perris R., Fang C.Matrix Biol. 21:461-470(2002) In vitro localization of TIGR/MYOC in trabecular meshwork extracellular matrix and binding to fibronectin.Filla M.S., Liu X., Nguyen T.D., Polansky J.R., Brandt C.R., Kaufman P.L., Peters D.M.Invest. Ophthalmol. Vis. Sci. 43:151-161(2002) Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.Proteomics 4:454-465(2004) Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells.Ambesi A., Klein R.M., Pumiglia K.M., McKeown-Longo P.J.Cancer Res. 65:148-156(2005) Differential analysis of site-specific glycans on plasma and cellular fibronectins application of a hydrophilic affinity method for glycopeptide enrichment.Tajiri M., Yoshida S., Wada Y.Glycobiology 15:1332-1340(2005) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A novel role for fibronectin type I domain in the regulation of human hematopoietic cell adhesiveness through binding to follistatin domains of FLRG and follistatin.Maguer-Satta V., Forissier S., Bartholin L., Martel S., Jeanpierre S., Bachelard E., Rimokh R.Exp. Cell Res. 312:434-442(2006) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.Proteomics 8:1346-1361(2008) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) A strategy for precise and large scale identification of core fucosylated glycoproteins.Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.Mol. Cell. Proteomics 8:913-923(2009) Regulation of p38 MAP kinase by anastellin is independent of anastellin's effect on matrix fibronectin.You R., Klein R.M., Zheng M., McKeown-Longo P.J.Matrix Biol. 28:101-109(2009) Resveratrol-induced changes of the human adipocyte secretion profile.Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., Mariman E.C., Renes J.J. Proteome Res. 11:4733-4743(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. 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. Biol. 276:177-187(1998) NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis.Fattorusso R., Pellecchia M., Viti F., Neri P., Neri D., Wuethrich K.Structure 7:381-390(1999) Solution structure of a pair of modules from the gelatin-binding domain of fibronectin.Bocquier A.A., Potts J.R., Pickford A.R., Campbell I.D.Structure 7:1451-1460(1999) The hairpin structure of the (6) F1(1) F2(2) F2 fragment from human fibronectin enhances gelatin binding.Pickford A.R., Smith S.P., Staunton D., Boyd J., Campbell I.D.EMBO J. 20:1519-1529(2001) NMR structure of human fibronectin EDA.Niimi T., Osawa M., Yamaji N., Yasunaga K., Sakashita H., Mase T., Tanaka A., Fujita S.J. Biomol. NMR 21:281-284(2001) Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors.Briknarova K., Aakerman M.E., Hoyt D.W., Ruoslahti E., Ely K.R.J. Mol. Biol. 332:205-215(2003) Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper.Schwarz-Linek U., Werner J.M., Pickford A.R., Gurusiddappa S., Kim J.H., Pilka E.S., Briggs J.A., Gough T.S., Hoeoek M., Campbell I.D., Potts J.R.Nature 423:177-181(2003) Crystal structure of the tenth type III cell adhesion module of human fibronectin.Dickinson C.D., Veerapandian B., Dai X.-P., Hamlin R.C., Xuong N.-H., Ruoslahti E., Ely K.R.J. Mol. Biol. 236:1079-1092(1994) 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.Leahy D.J., Aukhil I., Erickson H.P.Cell 84:155-164(1996) Crystal structure of a heparin- and integrin-binding segment of human fibronectin.Sharma A., Askari J.A., Humphries M.J., Jones E.Y., Stuart D.I.EMBO J. 18:1468-1479(1999) Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates.Gao M., Craig D., Lequin O., Campbell I.D., Vogel V., Schulten K.Proc. Natl. Acad. Sci. U.S.A. 100:14784-14789(2003) Interdomain association in fibronectin insight into cryptic sites and fibrillogenesis.Vakonakis I., Staunton D., Rooney L.M., Campbell I.D.EMBO J. 26:2575-2583(2007) The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin -- a tale with a twist.Rudino-Pinera E., Ravelli R.B., Sheldrick G.M., Nanao M.H., Korostelev V.V., Werner J.M., Schwarz-Linek U., Potts J.R., Garman E.F.J. Mol. Biol. 368:833-844(2007) Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains.Bingham R.J., Rudino-Pinera E., Meenan N.A.G., Schwarz-Linek U., Turkenburg J.P., Hoeoek M., Garman E.F., Potts J.R.Proc. Natl. Acad. Sci. 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.

Other Notes

Small volumes of FN1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for FN1 purchase

MBS955729 is a recombinant protein targeting FN1. Also known as Recombinant Human Fibronectin. Host: E Coli.

Additional Details

NCBI/Uniprot data below describe general gene information for FN1. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
UniProt Protein Name
Fibronectin
UniProt Synonym Protein Names
Cold-insoluble globulin; CIG
Protein Family
UniProt Gene Name
FN1
UniProt Synonym Gene Names
FN; FN; CIG
UniProt Entry Name
FINC_HUMAN
NCBI Protein Information
fibronectin

NCBI Summary for FN1

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]
Show more

UniProt Comments for FN1

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.
Show more

Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

Request a Quote

Please fill out the form below and our representative will get back to you shortly.

MBS000000
Contact Us

Please fill out the form below and our representative will get back to you shortly.

MBS000000