Homocysteine (Hcy) is a thiol-containing amino acid formed from methionine during S-adenosylmethionine-dependent transmethylation reactions. It has been demonstrated that even mild or moderately elevated levels of Hcyalso increase the risk of atherosclerosis of the coronary, cerebral andperipheral arteries and cardiovascular disease. And currently the hcy level isregarded as the biomarker for cardiovascular disease diagnosis all over the world.
Cystathionine gamma-lyase (CGL),or cystathionase (CSE, EC 18.104.22.168) , the enzyme participating in the synthesis of cysteine, catalyzes cystathionine deamination action, and form cysteine, alpha ketone butyric acid and NH3. In some bacteria and mammals, including humans, this enzyme takes part in generating hydrogen sulfide. Hydrogen sulfide is one of a few gases that was recently discovered to have arole in cell signaling in the body.
α-Methyl-glucuronidase 115A, Recombinant (Bacteroides ovatus)
Creative Enzymes uses its expertise in enzyme manufacturing to supply customers enzymes using for life science research and production of medicines, food, alcohol, beer, fruit juice, fabric, paper, leather goods, etc.
Our products are used worldwide in academic, commercial, and government laboratories in diverse applications, including basic research, drug discovery, cancer research, infectious disease research, microbiology, and personalized medicine. As a reliable supplier, Creative Enzymes supplies the products of high quality and competitive cost performance. We cooperate with a large number of satisfied customers in corresponding fields all over the world.
Creative Enzymes is customer-oriented. Our staff are always devoting themselves to provide quality products and considerate services to the customers. Some of our products are also unique in the field. Choosing our products means choosing high return.
For further development, Creative Enzymes warmly welcomes corresponding researchers to contact us for exploiting new enzymes together.
Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processes such as angiogenesis, intimal hyperplasia, atherosclerosis and aneurysms. Recently, MMPs have been linked to neurodegenerative diseases such as Alzheimer's, and amyotrophic lateral sclerosis (ALS). Natural inhibitors of MMPs, tissue inhibitor of matrix metalloproteinases (TIMPs) exist and synthetic inhibitors have been developed which offer hope of new treatment options for these diseases.
Acetyl-CoA Carboxylase (ACC) regulates the metabolism of fatty acids. This enzyme catalzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl CoA. There are two main isoforms of Acetyl-CoA carboxylase expressed in mammals, Acetyl-CoA carboxylase 1 (ACACA) and Acetyl-CoA carboxylase 2 (ACACB). ACACA has broad tissue distribution but is enriched in tissues critical for fatty acid sythesis such as adipose tissue. ACACB is enriched in tissues such as skeletal muscle and heart that are critical for fatty acid oxidation. The Acetyl-CoA Carboxylase enzymes are activated by Citrate, glutamate, and dicarboxylic acids and negatively regulated by long and short chain fatty acyl CoAs. Because of thier roles in fatty acid metabolism and oxidation, ACACA and ACACB are therapeutic targets for treating obesity and metabolic syndrome disorders.
Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications, whose wild-type (WT) version cleaves after T, A, S, and V residues. The M190A (Met190 → Ala190) mutant of aLP has different cleavage specificities, and cleaves after M, F, and L residues. Both the WT and M190A forms of aLP geneRate peptides of similar average length as trypsin.