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Papain is a cysteine protease of the peptidase C1 family.
| Molecular Weight | 226.23 |
| Formula | C9H14N4O3 |
| CAS Number | 9001-73-4 |
| Solubility (25°C) | Soluble in water |
| Storage | 2-8°C, protect from light, dry, sealed |
| Related Enzymes & Coenzymes Products |
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| Trypsin (bovine pancreas)
Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. |
| Neuraminidase
Neuraminidase is often used in biochemical studies. Neuraminidase cleaves α-ketosidic linkage between the sialic (N-acetylneuraminic) acid and an adjacent sugar residue. |
| Galactose oxidase
Galactose oxidase is a type II copper metalloenzyme, and it containing a single polypeptide. Galactose oxidase catalyzes two-electron oxidation of primary alcohols to their corresponding aldehydes, coupling with the reduction of dioxygen to hydrogen peroxide. Galactose oxidase is often used in biochemical studies. |
| L-Lactic dehydrogenase (rabbit muscle)
L-Lactic dehydrogenase is an enzyme that catalyzes the conversion of lactate to pyruvate. L-Lactic dehydrogenase also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids. L-Lactic dehydrogenase is used in the determination of pyruvate (used in conjunction with reduced coenzyme) and in the diagnosis of myocardial infarction and leukemia. |
| Lysostaphin
Lysostaphin is an antistaphylococcal agent. Lysostaphin has activities of three enzymes namely, glycylglycine endopeptidase, endo-β-N-acetyl glucosamidase and N-acteyl muramyl-L-alanine amidase. Lysostaphin specifically degrades bacteria such as Staphylococcus aureus whose cell wall has a glycine peptide bond structure, and achieves sterilisation by cleavage of its cell wall. |
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