fibrinogen

Fibrinogen is a heterodimeric protein that can be cleaved by thrombin. Fibrinogen is a potential marker for cardiovascular disease and plays an important role in metabolism. Its absence can cause fibrinogenemia.

H-D-Phe-Pip-Arg-pNA dihydrochloride (S-2238 dihydrochloride), a chromogenic substrate, mimics the N-terminal fragment of the A alpha chain of fibrinogen, the native substrate of thrombin. Specifically designed for thrombin detection, it is employed for quantifying antithrombin-heparin cofactor (AT-III) and is characterized by its sensitivity, accuracy, and ease of implementation.

GPRP acetate (Pefabloc FG) is fibrinogen-related peptides, which inhibit the interaction of fibrinogen with the platelet membrane glycoprotein IIbIIIa complex (GPIIbIIIa).

γ-Fibrinogen377-395 TFA is an inhibitory peptide derived from fibrinogen, which also functions as a fibrinogen epitope. It effectively blocks microglial activation and impedes fibrin-Mac-1 interactions in vitro. Additionally, it exhibits in vivo efficacy by suppressing experimental autoimmune encephalomyelitis (EAE) in mice. This compound has applications in researching multiple sclerosis (MS) and other neuroinflammatory diseases linked to blood-brain barrier disruption and microglial activation [1].

γ-Fibrinogen377-395 is a peptide derived from fibrinogen, functioning both as an inhibitory molecule and an epitope. It inhibits microglial activation, disrupts fibrin-Mac-1 interactions in vitro, and mitigates experimental autoimmune encephalomyelitis (EAE) in murine models in vivo. This compound is relevant for research into multiple sclerosis (MS) and other neuroinflammatory disorders characterized by blood-brain barrier compromise and microglial activation [1].

Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen, a soluble plasma protein and cofactor in platelet activation, is converted to fibrin in a thrombin-catalyzed reaction.

Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen-Binding Peptide binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation, and also inhibits the adhesion of platelets to vitronectin

Fibrinogen Binding Inhibitor Peptide, a synthetic dodecapeptide, represents the specific platelet receptor recognition site of the human fibrinogen g-chain (residues 400-411).

Arg-Gly-Asp-Ser (RGDS peptide) is a conserved tetrapeptide sequence found on fibronectin, fibrinogen α, and von Willebrand factor. It binds to integrins on the cell surface, inhibiting thrombin-induced platelet-fibrinogen interaction.

Bivalirudin (BG-8967) is a reversible inhibitor of α- and ζ-thrombin (Kis = 2.56 and 1.84 nM, respectively), enzymes that exhibit high fibrinogen-clotting activities.

Arg-Gly-Glu-Ser acetate is a RGD related peptide that is a control for the RGDS activity of fibrinogen binding to activated platelets.

Angstrom6 (A-6 peptide) is an 8 amino acid peptide derived from single chain urokinase fibrinogen activator (scuPA) that interferes with the uPA uPAR cascade and abrogates the downstream effects.Angstrom6 has antitumor activity and inhibits tumor cell migration, invasion, and metastasis by binding to CD44 and modulating CD44-mediated cell signaling.

GPRP (Gly-Pro-Arg-Pro) is a fibrin polymerization inhibitor that inhibits the interaction between fibrinogen and the platelet membrane glycoprotein IIb IIIa complex (glycoprotein IIb IIIa receptor).

H-D-Phe-Pip-Arg-pNA (S-2238) acetate is a chromogenic substrate based on the N-terminal fragment of the A alpha chain of fibrinogen, the physiological target of thrombin. As a specific indicator of thrombin activity, it is utilized to quantify thrombin. This assay ensures high sensitivity, accuracy, and ease of execution.

H-D-Phe-Pip-Arg-pNA hydrochloride, a chromogenic substrate, mimics the N-terminal segment of the A alpha chain of fibrinogen, the native substrate of thrombin. It is specific to thrombin and is used for quantifying antithrombin-heparin cofactor (AT-III), enabling a sensitive, accurate, and straightforward AT-III assay.

Arg-Gly-Asp-Cys TFA serves as the binding motif through which fibronectin interacts with cell adhesion molecules. This compound has the ability to hinder platelet aggregation and fibrinogen binding.

Lys-Gln-Ala-Gly-Asp-Val (KQAGDV), the six carboxyl-terminal amino acids of the fibrinogen γ-chain, serves as a potent cell adhesion peptide via the α2bβ3 integrin and a strong adhesion ligand for smooth muscle cells (SMCs) [1] [2].

Arg-Gly-Glu-Ser TFA, an RGD-related peptide, serves as a control for evaluating the inhibitory activity of RGDS on fibrinogen binding to activated platelets.

K-Casein (106-116), bovine, is a peptide that impedes platelet aggregation and fibrinogen binding, significantly contributing to the pathophysiology of atherosclerosis [1].

Integrin Signaling Inhibitor mP13 is a compound that impedes both inside-out and outside-in integrin-mediated signaling processes, such as fibrinogen binding, platelet adhesion, and clot retraction [1].

RTDLDSLRTYTL is a ligand for αVβ6 integrin, exhibiting selective inhibition of fibronectin's binding to αVβ6 integrin with considerably less effect on the interactions between vitronectin and αVβ3 or αVβ5, as well as fibrinogen and αIIβ3 (IC50s = 0.02, >50, >50, and >50 µM, respectively). Additionally, it prevents HT-29 colon cancer cells from binding to fibronectin in a concentration-dependent fashion.

Fibrinopeptide A, human is a 16-residue short polypeptide cleaved from fibrinogen by thrombin. Fibrinopeptide A, human locates at the NH2-termini of the Aα chain.The conversion of monomeric fibrinogen into polymeric fibrin is mediated by thrombin, which b

Fibrinopeptide A, human (FPA), is a 16-residue polypeptide cleaved from the N-terminal Aα region of fibrinogen by thrombin.

Fibrinopeptide A, human acetate (Human fibrinopeptide A acetate) is a 16-residue short polypeptide cleaved from fibrinogen by thrombin. Fibrinopeptide A (FPA) is produced from the N-terminal Aα region of fibrinogen protein, on cleavage by thrombin.