Fibronectin Fragments and Analogs

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A8052 Arg-Gly-Asp ≥97% (TLC) Primary sequence involved with the binding of proteins to cell surfaces
A9041 Arg-Gly-Asp-Ser ≥95% (HPLC)  
A6677 Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro ≥97% (HPLC) Inhibits fibronectin binding to fibroblasts.
A5686 Arg-Gly-Glu-Ser acetate salt ≥95% (HPLC) Inhibitor of platelet aggregation
F3667 Fibronectin Adhesion-promoting Peptide ≥95% (HPLC)  
F3542 Fibronectin Fragment III1-C human recombinant, expressed in E. coli, lyophilized powder, ≥90% (SDS-PAGE) Promotes cross-linking of fibronectin to form matrix fibril-like multimers.
F0162 Fibronectin Proteolytic Fragment from human plasma lyophilized powder, 45 kDa Fibronectin 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. Proteolytic fragments of fibronectin plays a vital role in mononuclear phagocyte function.
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.
F0287 Fibronectin Proteolytic Fragment from human plasma lyophilized powder, 70 kDa Fibronectin 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. Proteolytic fragments of fibronectin plays a vital role in mononuclear phagocyte function.
F9911 Fibronectin Proteolytic Fragment from human plasma lyophilized powder, 30 kDa Fibronectin 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. Proteolytic fragments of fibronectin plays a vital role in mononuclear phagocyte function.
F5007 Fibronectin Type III Connecting Segment Fragment 1-25 ≥90% (HPLC) Fibronectin Type III Connecting Segment (IIICS) is responsible for melanoma cell adhesion. It is the predominant binding site of integrin α4β1, which is mediated through the aspartic acid residue present at position 21. Studies in chicken show that alternative splicing in this region during development of the peripheral nervous system, is essential for the control cell-cell adhesion.
G4391 Gly-Arg-Gly-Asp-Ser ≥97% (HPLC) Gly-Arg-Gly-Asp-Ser inhibits metastasis in syngeneic mice or in mice lacking platelet function, when co-injected with B16-Fl0 melanoma cells.
G1269 Gly-Arg-Gly-Asp-Ser-Pro-Lys ≥97% (HPLC) Fibronectin analog that binds to integrins.
G5646 Gly-Arg-Gly-Asp-Thr-Pro ≥97% (HPLC) Inhibits cell attachment of fibronectin, vitronectin, and Type I collagen.
S3771 Ser-Asp-Gly-Arg-Gly ≥90% (HPLC) Reverse sequence of Gly-Arg-Gly-Asp-Ser, which does not appear to affect integrin function.