fibrinogen

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 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 Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen, a soluble plasma protein, is a cofactor in platelet activation. It is converted

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 (Bovine) is a molecule selectively proteolyzed, assembling into a fibrin clot upon thrombin 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).

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.

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.

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

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, H-D-Phe-Pip-Arg-pNA dihydrochloride is employed for the quantification of antithrombin-heparin cofactor (AT-III). The AT-III assay utilizing this substrate is characterized by its sensitivity, accuracy, and ease of implementation.

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

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 cell adhesion peptide via the α2bβ3 integrin. It is a potent adhesion ligand for smooth muscle cells (SMCs) [1] [2].

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

[Glu1]-Fibrinopeptide B, a derivative of fibrinopeptide B amino acid residues 1-14, originates from human fibrinopeptide B (hFpB). hFpB is a proteolytic cleavage product of the fibrinogen B beta-chain, specifically generated by thrombin, which plays a significant role in activating neutrophils (PMN), monocytes, and fibroblasts.

Arg-Gly-Asp-Cys is the binding motif of fibronectin and cell adhesion molecules, which can inhibit platelet aggregation and fibrinogen binding.

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.

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.

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 displays specificity towards thrombin and is employed for quantifying antithrombin-heparin cofactor (AT-III). The utilization of H-D-Phe-Pip-Arg-pNA hydrochloride in the AT-III assay enables a sensitive, accurate, and straightforward measurement process.

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

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

Fibrinopeptide A, human 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.

Arg-Gly-Glu-Ser 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.

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 B (FPB) is produced during the cleavage of fibrinogen, by thrombin, to fibrin monomer.

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

Gly-Pro-Arg-Pro Acetate, an inhibitor of fibrinogen aggregation, acts by binding to fibrinopeptide A.