A tetrapeptide found on fibronectin

RGDS Peptide – 25 mg

Brand:
Cayman
CAS:
91037-65-9
Storage:
-20
UN-No:
Non-Hazardous - /

Fibronectin is an extracellular matrix protein which binds other proteins and interacts with cells, serving roles in cell adhesion, migration, and signaling.{5588} Like vitronectin and collagen, fibronectin contains a conserved tripeptide sequence, Arg-Gly-Asp (RGD) to associate with integrins on the cell surface.{3775} RGDS peptide is a tetrapeptide found on fibronectin, fibrinogen α, and von Willebrand factor, but not vitronectin or collagen.{25165,25162} RGDS interacts with α5β1 and αVβ3 integrins.{25166} This tetrapeptide interferes with the attachment of cells to fibronectin-coated surfaces (Ki = 0.6 mM).{25165,25162} It also blocks the attachment of certain pathogens to cells.{25163,25164} RGDS peptide inhibits thrombin-induced binding of platelets to fibronectin, fibrinogen α, and von Willebrand factor (IC50 = ~10 μM).{25165,25167,25168} The interaction of RGDS peptide with cell surface integrins alters intracellular signaling in ways that are cell- and stimulus-specific.{25170,25169}  

 

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Description

A tetrapeptide found on fibronectin, fibrinogen α, and von Willebrand factor, but not vitronectin or collagen; interacts with α5β1 and αVβ3 integrins, blocking the attachment of cells to fibronectin-coated surfaces (Ki = 0.6 mM); inhibits adhesion of platelets to fibronectin, fibrinogen α, and von Willebrand factor (IC50 = ~10 μM)

Formal name: L-arginylglycyl-L-α-aspartyl-L-serine

Synonyms:  Fibronectin Inhibitor|H-Arg-Gly-Asp-Ser-OH

Molecular weight: 433.4

CAS: 91037-65-9

Purity: ≥95%

Formulation: A crystalline solid

Product Type|Biochemicals|Peptides||Product Type|Biochemicals|Receptor Pharmacology||Research Area|Cardiovascular System|Blood|Acute Phase Reactants||Research Area|Cardiovascular System|Blood|Coagulation & Hemostasis||Research Area|Cardiovascular System|Blood|Serum Proteins||Research Area|Cell Biology|ECM & Adhesion Molecules||Research Area|Immunology & Inflammation||Research Area|Infectious Disease

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