Protease

Leucine Aminopeptidase, Porcine (EC 3.4.11.1) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. Leucine Aminopeptidase, Porcine (EC 3.4.11.1) rapidly catalyzes the hydrolysis of leucine containing peptides and also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins.

Carboxypeptidase G, Pseudomonas sp. (EC 3.4.17.11) is a lysosomal thiol-dependent protease that stepwise cleaves γ-glutamylpteroyl polyγ-glutamic acid to generate pteroyl-α-glutamic acid (folic acid) and free glutamic acid. Carboxypeptidase G is highly specific for the γ-glutamyl bond but not for the C-terminal amino acid of the leaving group. Carboxypeptidase G can be activated by Zn²⁺ ions.

Protease, Streptomyces griseus, exhibits broad substrate specificity. Its active site consists of one aspartic acid residue, one histidine residue, and one serine residue. Protease tends to hydrolyze the peptide bond on the carboxyl side of glutamate or aspartate.

HIV-1 Protease is synthesized as part of a large Gag-Pol precursor protein. HIV-1 Protease is responsible for its own release from the precursor and the processing of the Gag and Gag-Pol polyproteins into the mature structural and functional proteins required for virus maturation.

IdeS protease is an IgG-specific endopeptidase, which is highly specific for the lower hinge region of IgG. IdeS protease represses innate immune responses to promote streptococcal survival in an inflammatory environment.

Elastase (high purity) is a serine protease that hydrolyzes proteins and peptides.

Protease (O-glycan Cleaving) is recombinantly expressed from E.coli and contains a His tag. Protease (O-glycan Cleaving) is an O-glycan-dependent protease that digests proteins carrying mucin-type O-glycans, including sialylated substrates, glycosylated Ser and Thr residues at the N terminus. Protease (O-glycan Cleaving) digests a variety of O-glycan structures, including sialylated glycosylated core 1 and core 2 structures and Tn antigen. Protease (O-glycan Cleaving) does not digest terminally modified serine or threonine residues, nor does it digest N-glycosylation sites on glycoproteins.

Protease (Fab Cleaving) is a serine protease expressed recombinantly in E.coli with a 6×His tag at the C-terminus. Protease (Fab Cleaving) specifically digests human IgG1 at a single site above the hinge, generating intact Fab and Fc fragments within two hours without reducing conditions.

Chitinase is a chitin-targeting enzyme with chitin hydrolysis activity. Chitinase inhibits chitin-induced innate type 2 inflammation in the lung. Chitinase augments chitin-free, allergen-induced Th2 inflammation. Chitinase mediates effector functions of IL-13.

Prolylendopeptidase, myxococcus xanthus (PEP-Mx) is an endopeptidase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture.

Methionine aminopeptidase is a kinase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture.

Dipeptidyl peptidase VII (human) is a peptidase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture.

Dipeptidyl peptidase III (human) is a hydrolase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture.

Dipeptidyl peptidase IX (human) is a hydrolase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture.

Oligopeptidase is a peptidase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture.

Lipase (MS grade) catalyzes the hydrolysis of triacylglycerols to release long-chain fatty acids in a site-specific manner. Lipase (MS grade) is involved in a variety of biological processes, from fat metabolism to cell signaling and inflammation, and can be used to study diseases such as pancreatic insufficiency, celiac disease and cystic fibrosis.

Prolyl Endopeptidase, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. Prolyl Endopeptidase can be used for study of neuropsychiatric diseases such as stress disorder, depression, and schizophrenia.

Endopeptidase, arctic marine microbial (ArcticZymes Proteinase), a proteinase, is used for the digestion of chromatin, thus releasing naked DNA. As it is thermolable, it can be inactivated at temperatures compatible with RNA integrity and DNA as double strands.

Protease for flavors is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Alkalophilic Proteinase, Streptomyces sp is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.