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F0162 Sigma

Fibronectin Proteolytic Fragment from human plasma

lyophilized powder, 45 kDa

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Description

Application

Fibronectin protelytic fragments can be used for mapping regions, functions and activities of fibronectin. This fragment is adjacent to the N-terminal domain, containing the only gelatin binding site. It is an acidic isolectric point, does not bind to heparin, and is resistant to proteolysis because of intrachain disulfide bonding. These disulfide bonds are essential for binding to gelatin. The fragment will bind to C1q, but not to fibrin.

Caution

The product should be stored at -20°C.

Packaging

0.5 mg in glass bottle

Preparation Note

This product is lyophilized from phosphate buffered saline with sucrose as a cryoprotectant. The source material has tested negative for antibody to HIV, HCN, and HBsAg. It is soluble in water at 0.5 mg/mL and yields a clear to slightly hazy solution.

Biochem/physiol Actions

Fibronectins are high molecular weight glycoproteins with two subunits joined by a disulfide bond to form the dimer. The fragments are obtained using protelytic enzymes. This 45 kDa gelatin binding fragment is obtained through trypitc digestion of the N-terminal 70 kDa fragment, which is produced by Cathespin D digestion.

This fragment has an acidic pI (4.9-5.3) and does not bind to heparin. This domain is resistant to proteolysis due to intrachain disulfide bonding and the attached carbohydrate. The intrachain disulfide bonds are essential for binding to gelatin, while the complex, branched, asparagine-linked carbohydrate is not. This fragment binds to C1q, but not to fibrin.

Price and Availability


Amplified Detection

All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

Symbol 
GHS07  GHS07
Signal word 
Warning
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles

Articles

Extracellular Matrix Proteins and tools for cell culture optimization

Animal cells and tissue culture techniques are constantly improved to optimize in vitro cell culture conditions. Extracellular Matrix (ECM) proteins coating, chemical or physical modification of the ...
Keywords: Adhesion, Angiogenesis, Apoptosis, Asymmetric synthesis, Cancer, Cell attachment, Cell culture, Cell proliferation, Coagulation, Endocrinology, Growth factors, Hormones

Fibronectin Cell Attachment Protocol

Freezing and thawing of reconstituted fibronectin is not recommended as breakdown of protein will occur.
George Sitterley
BioFiles 2008, 3.8, 9.
Keywords: Phase transitions

Peer-Reviewed Papers
15

References

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Description

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F9911 Fibronectin Proteolytic Fragment from human plasma, lyophilized powder, 30 kDa
F0287 Fibronectin Proteolytic Fragment from human plasma, lyophilized powder, 70 kDa

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