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F2518

Sigma-Aldrich

Human Fibronectin

from human foreskin fibroblasts, powder, suitable for cell culture

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Synonym(s):
Fibronectin
EC Number:
289-149-2
MDL number:
MFCD00131062
UNSPSC Code:
12352202
NACRES:
NA.75

product name

Fibronectin human foreskin fibroblasts, lyophilized powder, suitable for cell culture

biological source

human foreskin fibroblasts

Quality Level

200

product line

BioReagent

form

lyophilized powder

mol wt

~550 kDa

packaging

pkg of 0.5 mg

technique(s)

cell culture | mammalian: suitable

surface coverage

1‑5 μg/cm2

impurities

Human Source, none detected (HCV)
 Human Source, none detected (HIV)
 Human Source, none detected (HTLV)
 Human Source, none detected (HbSAg)
 Microbial Contamination, passes test

solubility

H2O: 1 mg/mL at 37 °C (Store reconstituted solution in working aliquots at -20°C or lower.)

NCBI accession no.

NM_212482.4

UniProt accession no.

P02751

Binding Specificity

Peptide Source: Collagen

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... FN1(2335)

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General description

Fibronectin 1 (FN1) is a glycoprotein of the extracellular matrix that is coded by FN1 gene. It is expressed in the plasma and at the cell surface. It is mapped to human chromosome 2q35. Fibronectin is mostly synthesized by fibroblasts and endothelial cells.It is an adhesive glycoprotein, predominant in extracellular matrix (ECM) and is widely distributed in tissue and blood. The fibronectin structure consists of blocks of repeating peptide sequences that are homologous and form functional units arranged linearly ontwo subunit arms.

Application

Epithelial cells, mesenchymal cells, neuronal cells, fibroblasts, neural crest cells, endothelial cells
Fibronectin human foreskin fibroblasts has been used in extracellular matrix binding assay and probiglycan and cleavage assays. It has also been used in ectoderm (neuronal) differentiation and in the preparation of a semi-solid growth medium.

Biochem/physiol Actions

Fibronectin 1 (FN1) participates in cell adhesion, growth, migration, wound healing, blood coagulation and metastasis. Mutations in FN1 results in glomerulopathy. It plays an important role in cell attachment and spreading, control of cell cytoskeleton, morphology and differentiation. FN1 is also involved in extracellular matrix formation, hemostasis and thrombosis. Fibronectin production by normal human foreskin fibroblasts has been shown to improve two-fold after glucocorticoid treatment.

Features and Benefits

  • Fibronectin is isolated from human foreskin fibroblasts maintained in serum-free medium.
  • It can be used as a cell attachment factor for various cell types, including epithelial, mesenchymal, neuronal, neural crest, endothelial cells, and fibroblasts.
  • The starting material is tested and found negative for HIV and HBsAg.
  • The product is soluble in sterile water, yielding a clear, colorless solution.
  • It can be stored at -20°C for at least three years.

Caution

Vortexing, excessive agitation, repeated freezing and thawing of reconstituted fibronectin are not recommended.

Physical form

Lyophilized in CAPS buffered saline

Preparation Note

dialyzed against chloroform

Reconstitution

Store reconstituted solution in working aliquots at -20°C or lower.

Analysis Note

Protein homogeneity is evaluated by immunoelectrophoresis.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Fibronectin binds and enhances the activity of bone morphogenetic protein 1.
Huang G, et al.
The Journal of Biological Chemistry (2009)
Artificial biomaterials for urological tissue engineering
Farhat WA and Geutjes, PJ
Journal of Separation Science (2009)
Construction and characterization of a multilayered gingival keratinocyte culture model: the TURK-U model.
Gursoy U K, et al.
Cytotechnology, 68(6), 2345-2354 (2016)
Fibronectin: a brief overview of its structure, function, and physiology
Proctor RA
Reviews of Infectious Diseases, 317?321-317?321 (1987)
Ramesh B Kasetti et al.
Scientific reports, 7(1), 14951-14951 (2017-11-04)
Increased synthesis and deposition of extracellular matrix (ECM) proteins in the trabecular meshwork (TM) is associated with TM dysfunction and intraocular pressure (IOP) elevation in glaucoma. However, it is not understood how ECM accumulation leads to TM dysfunction and IOP
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