collagen

Fasudil (HA-1077) is a potent inhibitor of ROCK1, PKA, PKC, and MLCK.

Fasudil hydrochloride (HA-1077) is a potent inhibitor of ROCK1, PKA, PKC, and MLCK with Ki of 0.33 μM, 1.0 μM, 9.3 μM and 55 μM, respectively.

L-Ascorbic acid (Vitamin C) is a natural product that is a potent reducing agent and antioxidant. L-Ascorbic acid functions in fighting bacterial infections, in detoxifying reactions, and in the formation of collagen. L-Ascorbic acid is used in the treatment of scurvy.

Collagen proline hydroxylase inhibitor-1 exhibits antifibroproliferative activity.

safironil is a novel antifibrotic compound and a competitive inhibitor of collagen synthesis. safironil inhibited in vitro experiments on fibroblast activation monitored by collagen I mRNA or smooth muscle alpha-actin levels, and fibrogenesis as judged by type I and type III collagen and laminin production. safironil had no effect on the size of liver granulomas without altering total hydroxyproline, but altered the pattern of fibrosis by increasing type III and decreasing type I collagen deposition.

Ethyl 3,4-dihydroxybenzoate (EDHB): a prolyl hydroxylase inhibitor attenuates acute hypobaric hypoxia mediated vascular leakage in brain.

Collagen proline hydroxylase inhibitor is an inhibitor collagen proline hydroxylase and useful for antifibrotic proliferative agents.

Collagen type IV alpha1 (531-543) is a protein that in humans is encoded by the COL4A1 gene on chromosome 13. It is ubiquitously expressed in many tissues and cell types. COL4A1 is a subunit of type IV collagen and plays a role in angiogenesis.

Collagen-IN-1 (compound 3) is an ortho-carbonyl hydroquinone derivative that selectively inhibits collagen. It non-competitively inhibits agonist-induced platelet aggregation, with an IC50 value of 1.77 μM. Collagen-IN-1 reduces P-selectin expression, glycoprotein IIb IIIa activation, and the release of adenosine triphosphate and CD63 from platelets. This compound is promising for research into platelet-related thrombosis diseases [1].

Anti-Human Mouse denatured collagen type-I Antibody (XL313) is an IgG1, κ inhibitor derived from mice, targeting denatured collagen type-I in both human and mouse.

This is a peptide inhibitor of collagen fibrillar matrix assembly.

Collagen Type II Fragment is a peptide with anti-inflammatory properties that effectively inhibits collagen-induced arthritis (CIA) in mice. It is useful for research focused on inflammation and immunity [1].

Collagen, rat tail is a natural collagen from rat tail tendon, the main component is collagen type I. It can support cell attachment, proliferation and differentiation, and is commonly used in the preparation of cell culture substrates.

Bovine Type II Collagen (Collagen Type II,Bovine) is a homologous superhelical structure consisting of three identical α1(II) chains, and is a major component of animal cartilage. Type II collagen has a variety of biological activities, including maintaining cartilage tissue integrity, inducing immune tolerance, and stimulating chondrocyte growth and redifferentiation.

Type II collagen is composed of a triple helix of three identical α chains. These molecules associate to form a fibril that is stabilized by intermolecular crosslinks1. Damage to the fibrillar meshwork, made up of primarily type II collagen (z 90–95%), ma

Collagen, Type I, from bovine achilles tendon is a type I collagen derived from bovine achilles tendon, which is widely found in marine invertebrate tissues. Collagen, Type I, from bovine achilles tendon is the only component of collagen fibers that make up the dermis, and plays a major role in bone and connective tissue. connective tissues, and functions primarily by forming and maintaining the integrity of the skeleton.

Collagen-binding peptide is a conserved fibronectin peptide (FNIII-7,10) recognized for its importance in cellular interactions and tissue repair.

Collagenase Type II, an endopeptidic matrix metalloproteinase MMP-8 derived from the bacterium Clostridium histolyticum, preferentially degrades type I collagen and is commonly used in tissues requiring high digestive efficiency such as pancreas and liver.

Collagenase, Type VI (EC 3.4.24.3) is an enzyme specialized in degrading Type VI collagen, a component found in various tissues including skin, heart, blood vessels, cartilage, and the cell membranes in synovia. Excessive activity of this enzyme can lead to extracellular matrix disorders. Additionally, Collagenase, Type VI serves as a biomarker for tumor invasion and metastasis. It acts specifically on peptide bonds between proline and glycine. Exploiting this specificity, modified electrodes can be used to rapidly and sensitively detect its concentration levels in experiments.

Collagenase Type III, an endopeptide matrix metalloproteinase MMP-13 derived from the bacterium Clostridium histolyticum, preferentially degrades type III collagen and is commonly used in sensitive tissues such as breast, tumor, and uterus due to its mild activity.

Collagenase Type IV is an endopeptidic matrix metalloproteinase MMP-18 derived from the bacterium Clostridium histolyticum that primarily degrades collagen type IV and VII and is commonly used to break down basement membranes (e.g., neural tissue, renal tissue) because of its mild activity.

Collagenase Type I is an endopeptidic matrix metalloproteinase MMP-1 derived from the bacterium Clostridium histolyticum, which preferentially degrades type II collagen and is commonly used in tissues requiring high digestive efficiency, such as pancreas and liver.

Collagenase, Type VIII, has the capability to hydrolyze Type VIII collagen, and may be utilized in the study of atherosclerosis development. Type VIII collagen serves as a regulator of endothelial cell differentiation and angiogenesis, acts as a substrate for the adhesion and migration of cells such as smooth muscle cells, and may accumulate in atherosclerosis. Following the activation by endotoxins, the expression of Collagenase, Type VIII can reduce the production of Type VIII collagen, potentially inhibiting the progression of atherosclerosis.

Collagenase Type V, an endopeptidic matrix metalloproteinase MMP from the bacterium Clostridium histolyticum, can be used for islet tissue isolation.