proteinase

Proteinases are enzymes that catalyse the breakdown of proteins. Proteinases are involved in many biological functions, including the digestion of ingested proteins, the breakdown of old proteins, and cell signalling. They also facilitate the formation of new protein products.

Endopeptidase, arctic marine microbial (ArcticZymes Proteinase), is a protease utilized for chromatin digestion to release exposed DNA. Its thermal instability allows for deactivation at temperatures that maintain RNA integrity and are compatible with double-stranded DNA.

Aspartic acid proteinase is a proteolytic enzyme characterized by its catalytic activity mediated by two critical aspartic acid residues at the active site, facilitating the hydrolysis of protein peptide bonds.

Microbial neutral proteinase is a neutral protease derived from microorganisms, useful for cell and tissue dissociation.

Neutral Proteinase, derived from Bacillus sp., serves as a biocatalyst and is a pivotal enzyme in novel biocatalyst technology. Enzyme engineering focuses on improving reaction kinetics, substrate selectivity, and maintaining activity under challenging conditions (e.g., low or high pH). By incorporating stimuli-responsive modifications, dynamic control of enzyme activity can also be achieved.

Alkalophilic Proteinase, Streptomyces sp is a biocatalyst and a crucial enzyme in new biocatalyst technology. Enzyme engineering focuses on improving reaction kinetics, substrate selectivity, and activity under harsh conditions (e.g., low or high pH). By incorporating stimulus responsiveness into these enzyme modifications, dynamic control over activity is also achieved.

Proteinase K (Protease K) (NGS grade) (EC 3.4.21.64) is a serine protease known for its high enzyme activity and broad substrate specificity. It preferentially cleaves ester and peptide bonds adjacent to hydrophobic, sulfur-containing, and aromatic amino acids at the C-terminal. It is commonly used in protein degradation to produce short peptides. This product is NGS grade, free of Nickase.

Endoproteinase Arg-C is a serine endopeptidase capable of hydrolyzing peptide bonds at the carboxyl side of arginyl residues, and exhibits both esterase and amidase activities. It can be isolated from Clostridium histolyticum. Endoproteinase Arg-C is of mass spectrometry grade and is applicable for peptide mapping, sequence analysis, and cell isolation.

Endoproteinase Lys-N (MS grade) is a protease that specifically cleaves peptide bonds at the N-terminal side of lysine residues.

Endoproteinase Asp-N (Asp-N) is a metalloprotease that specifically cleaves on the N-terminal side of aspartic acid and sulfoalanine residues.

Matrix metalloproteinase 3 is a biochemical reagent that functions as a biological material or organic compound, utilized in research related to life sciences.

Chondroitin sulfate (Chonsurid) is extracted from shark bone;Store the product in sealed, cool and dry condition

o-Phenanthroline (1,10-Phenanthroline) , a metal chelator, prevents the induction of chromosomal aberrations in streptozotocin-treated cells.o-Phenanthroline protects mammalian cells from hydrogen peroxide-induced gene mutation and morphological transformation.

o-Phenanthroline monohydrate (1, 10-Phenanthroline monohydrate) is an inhibitor of metallopeptidases, inhibits zinc-dependent hydrolysis of Fa-Gly-Leu-NH2 by B. subtilis neutral protease and B. thermoproteolyticus thermolysin.

Trigalacturonic acid is an oligosaccharide that inhibits proteinase activity in tomato plants (ED50 = 2.6 μg/plant).