Elastase is an enzyme from the class of proteases (peptidases) that break down proteins. It hydrolyzes peptide bonds, especially those adjacent to neutral amino acids. Hydrolyses elastin Digests hemoglobin, casein, and fibrin One unit will solublize 1 mg of elastin in 20 minutes at…

Collagenases degrade native helical collagen fibrils. It has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. Collagenase is used for tissue dissociation combined with other enzymes such as elastase, trypsin,…

Hyaluronidase is a glycoprotein containing 5% mannose and 2.17% glucosamine, it catalyzes the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- β-D-glucose and D-glucose residues in hyaluronate. Hyaluronidase from bovine testes is a tetramer consisting of 4 equal subunits with a…

Biliverdin Dihydrochloride is a bile pigment component. An oxidized metabolite of bilirubin caused when bilirubin reacts with reactive oxygen species. Biliverdin IX is composed of alpha, beta, gamma and delta isomers. Biliverdin dihydrochloride was found responsible for cytoprotection. It was…

Hyaluronidase is a glycoprotein containing 5% mannose and 2.17% glucosamine, it catalyzes the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- b-D-glucose and D-glucose residues in hyaluronate. Hyaluronidase from bovine testes is a tetramer consisting of 4 equal subunits with a…

Tight-binding, reversible, highly selective inhibitor of acid proteases (aspartyl peptidases), like pepsin, gastricsin, cathepsin E and D, renin, chymosin, bacterial aspartic proteinases and HIV proteases. Does not inhibit thiol proteases, neutral proteases or serine proteases. Widely used as a…

AEBSF hydrochloride is a covalent binding serine protease inhibitor, belongs to the family of irreversible sulfonyl fluoride inhibitors that block trypsin and chymotrypsin-type enzymes. Similar in structure to the commonly used inhibitor PMSF, AEBSF offers better solubility in water, lower…

Also known as bovine pancreatic trypsin inhibitor. Activity: Approx 6,000 KIU/mg Specificity: A broad range, competitive and reversible inhibitor of chymotrypsin, plasmin, trypsin, kallikrein and other serine proteases Solubility: Soluble in water (Stock solution: 10mM) A…

Potent anticancer compound. Anti-angiogenic. VEGF, VE-cadherin phosphorylation, matrix metalloproteinase and urokinase-plasminogen activator (uPA) inhibitor. Anti-inflammatory. NF-kappaB inhibitor. Modulates chronic inflammatory diseases, such as type 2 diabetes, rheumatoid arthritis, inflammatory…

Potent phenolic antioxidant found in grapes and red wine. Eicosanoid synthesis and platelet aggregation inhibitor. Estrogen receptor agonist. Chemopreventive. Specific inhibitor of cyclooxygenase-1 (COX-1). Anti-inflammatory. Ribonucleotide reductase and DNA synthesis. Arrests cell cycle at S/G2…

Acetyl-CoA is produced via beta-oxidation of fatty acids, via the metabolism of carbohydrates - glucose 6-phosphate to pyruvate to acetyl-CoA and via the catabolism of amino acids. Acetyl-CoA has a number of metabolic opportunities. It is metabolized in the tricarboxylic acid cycle to produce…

Trypsin consists of a single chain polypeptide of 223 amino acid residues. Member of the serine protease family Dissolves blood clots in its microbial form Treats inflammation in its pancreatic form Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues.…

Anticancer compound. Chemotherapeutic used in patients with cancer and advanced forms of Kaposi's sarcoma. Microtubule assembly stabilizer. Reversibly binds to polymerized tubulin. Anti-mitotic. Mitotic spindle assembly, chromosome segregation and cell division inhibitor. Induces cell cycle…

Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachiumalkaline phosphatase) (EC 3.4.21.64) is a non-specifc, broad spectrum serine protease that is isolated from the saprophytic fungus Tritirachium album. Proteinase K is routinely used for the purification of target…

Collagenases degrade native helical collagen fibrils. Plays an important role in connective tissue metabolism Produced by specific cells involved in repairs and remodeling processes Type II enzyme that contains greater clostripain activity Collagenase is used for collagen…

A serine proteinase used to inactivate RNAse and DNAse in RNA and DNA isolation protocols. Useful in the study of membrane and protein structure. Proteinase K is a highly active protease (MW 28,500 Da) isolated from the fungus Tritirachium album . The enzyme exhibits broad specificity on…

Collagenase is a protease which cleaves the triple-helical protein called collagen. There are three types of tissue collagenases, and these belong to the matrix metalloproteinases (MMP) family. Collagenase from Clostridium histolyticum has extensive use in biological studies, where it is used to…

Papain is a sulfhydryl protease from Carica papaya latex. Cleaves peptide bonds of basic amino acids, leucine, or glycine Hydrolyzes esters and amides One unit will hydrolyze 1.0 µmole of N-alpha-benzoyl-L-arginine ethyl ester (BAEE) per minute at 25°C and pH 6.2 Papain…

Potent platinum-based antineoplastic agent with wide spectrum anticancer activity. Anticancer compound. Forms inter- and intrastrand DNA adducts/crosslinks, consequently blocking DNA replication and transcription and inducing cell death. Shows antitumor activity in cisplatin resistant cell lines.…

A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond. Produced from 3x Crystallized chymotrypsinogen Used to treat pancreatic insufficiency Used in traumatology Chymotrypsin…

Potent phenolic antioxidant found in grapes and red wine. Eicosanoid synthesis and platelet aggregation inhibitor. Estrogen receptor agonist. Chemopreventive. Specific inhibitor of cyclooxygenase-1 (COX-1). Anti-inflammatory. Ribonucleotide reductase and DNA synthesis. Arrests cell cycle at S/G2…

Protease which cleaves specifically at the -COOH side of arginie and lysine. TPCK-treated Trypsin is a serine endopeptidate Trypsin is treated with TPCK to inactivate any remaining chymotryptic activity This type of trypsin is modified by acetyltion of the sigma-amino groups of lysine…

Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The…

Antihelminthic, molluscicide and trypanocidal agent that inhibits mitochondrial oxidative phosphorylation and anaerobic ATP production. Anticancer agent with antiproliferative activity in a broad spectrum of cancer cells. Targets and inhibits multiple signaling pathways, including STAT3, NF-kB,…

Ribonuclease A, and to a greater extent its oligomers and some homologs (such as onconase from frogs), have cytotoxic and cytostatic effects, particularly on cancer cells.This attribute has led to the development of onconase as a cancer therapeutic. Ribonuclease A is used to remove RNA from DNA…

Leupeptin is a modified tripeptide reversible protease inhibitor of trypsin-like proteases and some cysteine proteases including endoproteinase Lys-C, kallikrein, papain, thrombin, cathepsin B, cathepsins H and L, trypsin, calpain, trypsin8 and plasmin. Effective concentration is typically 10-100…

Potent, competitive and reversible cysteine, serine and threonine protease inhibitor. Inhibits calpain, kallikrein, trypsin, plasmin, papain and cathepsin B. Does not inhibit pepsin, elastase, renin, cathepsins A and D, thrombin or alpha-chymotrypsin. Used to protect against hearing loss caused by…

Pepstatin A is a reversible inhibitor of aspartic proteases, Inhibitor for pepsin, renin, cathepsin D, cathepsin G, and other acid proteases. It does not inhibit thiol proteases, neutral proteases or serine proteases. Pepstatin forms a 1:1 complex with acid proteases (carboxyl proteases). …

Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles)…

Diamide is used as a thiol oxidizing agent. It has also been used to titrate protein glutathiolation to discriminate from other oxidative protein modifications. Diamide treatment increased protein glutathiolation in a concentration-dependent manner and had comparably little effect on…

L-glutamic dehydrogenase is a pyridine nucelotide enzyme which catalyzes the reversible oxidative deamination of L-glutamate to α-keto-glutarate and ammonia. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway…

Naphthol AS-D chloroacetate is a substrate for histochemical localization of esterases.