|Related Categories||Application Index, Attachments Factors, Biochemicals and Reagents, Cell Biology, Cell Signaling Enzymes,|
|impurities||HIV and HBsAg, source material tested negative|
|Small proteolytic fragments, may contain traces|
|Gene Information||human ... FN1(2335)|
The proteolytic fragments can be used for mapping regions, functions, and activities of fibronectin.
Lyophilized from phosphate buffered saline with sucrose as a cryoprotectant
Fibronectin fragments are obtained from plasma fibronectin by using proteolytic enzymes. These fragments are useful tools for mapping regions within the fibronection molecule, which are responsible for specific binding to collagen and for other biologically relevant functions. The N-terminal 70 kDa fragment (Product No. F 0287) is obtained by Cathepsin D digestion. This fragment binds to both gelatin and heparin. Tryptic digestion of this 70 kDa fragment yields two peptides: the N-terminal 30 kDa heparin binding fragment (Product No. F9911) and a 45 kDa gelatin binding fragment (Product No. F 0162).
Fibronectin proteolytic fragment 30 kDa, the heparin binding fragment, is the N-terminus of fibronectin. This fragment has a basic pI (8.2–8.6) and is free ofcarbohydrate moieties. The fragment is rich in cystine residues, but has no free sulfhydryl groups. The amino acid sequence of this domain is composed of five disulfide-bonded loops. This fragment binds to heparin, fibrin, and collagen. The primary physiological role of this domain appears to be the binding of fibrin
Customers Also Viewed
recombinant, expressed in E. coli, lyophilized powder, ≥90% (SDS-PAGE)
lyophilized powder, BioReagent, suitable for cell culture
lyophilized powder, 45 kDa
lyophilized powder, 70 kDa
Certificate of Analysis
Freezing and thawing of reconstituted fibronectin is not recommended as breakdown of protein will occur.
BioFiles 2008, 3.8, 9.
Keywords: Phase transitions
Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy. Huff, S., et al. J. Biol. Chem. 269, 15563, (1994)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Need larger quantities for your development, manufacturing or research applications?