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.

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].

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

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

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].

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-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.

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

Arg-Gly-Asp-Cys acetate inhibits platelet aggregation and fibrinogen binding. Arg-Gly-Asp-Cys acetate is the binding motif of fibronectin to cell adhesion molecules.

Arg-gly-glu -Ser(TFA) is a RGD related polypeptide that controls the inhibition of fibrinogen binding to activated platelets by RGDS.

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.

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.

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

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.

FibrinopeptideB,human is a 14-amino acid polypeptide released from the amino terminus of the fibrinogen segment.

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.

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].

Thrombin is a trypsin-like serine protease that is encoded by the F2 gene in humans. Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). Thrombin in turn acts as a serine protease that converts soluble

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

pGlu-Pro-Arg-MNA monoacetate, a thrombin substrate modeled after a thrombin cleavage site in human fibrinogen, can be used for sensitive assays of antithrombin III activity.

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 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.