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Key Documents

Safety Information

ECM001

Sigma-Aldrich

Human Fibronectin

recombinant, expressed in HEK 293 cells, powder, suitable for cell culture

Synonym(s):

Fibronectin, CIG, Cold-insoluble globulin, FN

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.75

Pricing and availability is not currently available.

Product Name

Fibronectin human, recombinant, expressed in HEK 293 cells, lyophilized powder, suitable for cell culture

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

sterility

sterile

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

mol wt

259.5 kDa (The protein migrates as a higher band on SDS-PAGE due to glycosylation.)

packaging

pkg of 200 μg

technique(s)

cell culture | mammalian: suitable

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This Item
F2006F2518F0162
sterility

sterile

sterility

sterile

sterility

-

sterility

-

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

assay

≥95% (SDS-PAGE)

assay

≥85% (SDS-PAGE)

assay

-

assay

≥90% (SDS-PAGE)

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

recombinant

expressed in HEK 293 cells

recombinant

-

recombinant

-

recombinant

-

General description

Fibronectin (FN) is a glycoprotein with 5-9% carbohydrates present as N- and O-linked oligosaccharides.[1] It belongs to the ligand glycoprotein family. The FN gene is localized to human chromosome 2q35.[2] FN exists as two major isoforms, plasma-based soluble and extracellular matrix (ECM)-based insoluble form.[1] Fibronectin structure comprises repeats of FNI, FNII and FNIII repeats.[3] It also has fibrin-binding sites and exists as a dimer.[4] Alternative splicing of the FN1 gene leads to the generation of many isoforms.[1] This fibronectin protein is manufactured in human cells using an all-human production system with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports better stability of the protein in culture.

Application

Epithelial cells, mesenchymal cells, neuronal cells, fibroblasts, neural crest cells, endothelial cells.
Recommended for use as a cell culture substratum at 1-5 μg/cm2 or 0.5-50 μg/ml. Optimal concentration depends on cell type as well as the application or research objectives.
Fibronectin human has been used for coating cell culture plates for culturing endothelial progenitor cells.[5] It has also been used as a component of Dulbecco′s modified Eagle′s medium (DMEM) in the in vitro matrigel invasion assay of glioblastoma cells.[6]

Biochem/physiol Actions

Fibronectin (FN) is essential for embryonic development and mediates cell adhesion and migration functions.[2] It mediates apoptosis in nasopharyngeal carcinoma (NPC). The plasma FN regulates thrombosis.[1] Fibronectin functions as a ligand for the integrin receptor family[4] and contains collagen, glycoprotein and glycosaminoglycan binding sites.[7] Mutation in the FNI gene leads to an imbalance in the soluble and insoluble forms of fibronectin leading to glomerular deposits in hereditary kidney disease, glomerulopathy.[8] Missense mutations in the FN1 gene are implicated in the skeletal dysplasias disorder, Spondylometaphyseal dysplasias.[7]

Features and Benefits

  • Human-derived fibronectin
  • Produced through recombinant expression in HEK 293 cells
  • Low endotoxin levels
  • Absence of bacterial contamination

Physical form

Supplied as a powder, lyophilized from CAPS buffered saline.

Analysis Note

The biological activity of recombinant human fibronectin was tested in culture by measuring the ability of immobilized fibronectin to support adhesion of CHO cells.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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    The association between hyperhomocysteinemia and cerebral small vessel disease
    Yang Y, et al.
    International Journal of Clinical and Experimental Medicine, 12, 13877-13883 (2019)
    Jinting Wang et al.
    American journal of translational research, 9(10), 4502-4511 (2017-11-10)
    Fibronectin 1 (FN1) is a member of the glycoprotein family located on chromosome 2q35. It has been reported that FN1 is upregulated in many tumors, and its expression is negatively related to the prognosis and survival of cancer patients. Through
    Jeannette Huaman et al.
    Cells, 9(7) (2020-07-08)
    Fibronectin (FN1) is an extracellular matrix protein gaining increasing attention for its multifaceted roles in cancer progression. Using our recently established circulating tumor cell (CTC) lines, we had demonstrated increased FN1 expression and enhanced migration in CTC lines, in comparison
    Wing S To et al.
    Fibrogenesis & tissue repair, 4, 21-21 (2011-09-20)
    Fibronectin (FN) is a ubiquitous extracellular matrix (ECM) glycoprotein that plays vital roles during tissue repair. The plasma form of FN circulates in the blood, and upon tissue injury, is incorporated into fibrin clots to exert effects on platelet function
    Hsiang-Chi Tseng et al.
    Nature communications, 11(1), 4810-4810 (2020-09-25)
    Chimeric antigen receptor (CAR) therapy is a promising immunotherapeutic strategy for treating multiple refractory blood cancers, but further advances are required for solid tumor CAR therapy. One challenge is identifying a safe and effective tumor antigen. Here, we devise a

    Articles

    The extracellular matrix (ECM) and its attachment factor components are discussed in this article in relation to their function in structural biology and their availability for in vitro applications.

    The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues.

    Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

    Protocols

    Dilute fibronectin for cell attachment, varying per cell type. Coating protocol, products, and FAQs provided.

    Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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