Protease

Endoproteinase Glu-C (MS grade) is a serine proteinase. Endoproteinase GluC is able to hydrolyze some serpins and all classes of mammalian immunoglobulins.

Heparinase (Heparinase I) degrades heparin to oligosaccharide or unsaturated disaccharide. Heparinase can be used in the preparation of low molecular weight heparin (LMWH).

Cholinesterase, Horse serum infers to acetylcholinesterase (AChE) and butyryl cholinesterase (BChE). AChE and BChE catalyze the hydrolysis of 6-MAM to morphine.

Recombinant Kex2 protease is a membrane-bound, Ca²⁺-dependent serine protease. Recombinant Kex2 protease specifically recognize and cleave the carboxyl-terminal peptide bonds of dibasic amino acids.

Chymopapain is a non-specific proteo-glycanase derived from the papaya plant. Chymopapain has neurotoxicity when injected into nerve bundles. Chymopapain directly into the intervertebral disc caused disc narrowing due to dissolution of the extruded material. Chymopapain has the potential for the research of herniated lumbar discs.

Penicillin amidase, E. coli (Immobilized) (PGA) is an amidohydrolase commonly used in industrial biocatalysis. Penicillin amidase, E. coli (Immobilized) serves as a starting material in the synthesis of semi-synthetic penicillins. Penicillin amidase, E. coli (Immobilized) promotes the production of semi-synthetic β-lactam antibiotics, participates in peptide synthesis, and catalyzes the formation of chiral compounds. Penicillin amidase, E. coli (Immobilized) is regulated by temperature and phenylacetic acid in E. coli. In free E. coli, it participates in the assimilation of aromatic compounds as a carbon source. Penicillin amidase, E. coli (Immobilized) is hypothesized to act as a scavenging enzyme for phenylacetyl-containing compounds in microbial metabolism and is associated with bacterial quorum sensing.

Clostripain (Clostridiopeptidase B) is a thiol protease isolated from Clostridium histolyticum. Clostripain exhibits proteolytic activity as well as amidase-esterase activity. The specificity of Clostripain is primarily restricted to arginine residues, but it also shows minor hydrolytic activity toward most lysine-containing substrates. Clostripain catalyzes the ammonolysis of Carbobenzoxyarginyl methyl ester to generate various dipeptides.

Carboxypeptidase B (MS grade) is a peptide exonuclease that can specifically degrade peptide chains. Carboxypeptidase B (MS grade) is progressively degraded from the C-terminal to release free amino acids. Carboxypeptidase B (MS grade) hydrolyzes only peptide bonds with basic amino acids (such as arginine and lysine) as C-terminal residues.

Aspergillopepsin I (Aspergillus acid protease) is a metal-containing aspartic protease that catalyzes the hydrolysis of peptide bonds in soybean 7S globulin, soybean 11S globulin and various proteins, with broad specificity. Aspergillopepsin I is intended for use in wine production, where it hydrolyzes haze-forming proteins into small peptides to prevent turbidity during storage. Aspergillopepsin I can be used in studies related to soybean protein hydrolysis and wine production.

Trypsin/Lys-C complex protease (MS grade) combines Trypsin and Lys-C, two recombinant proteases, to achieve efficient peptide bond hydrolysis. Trypsin specifically cleaves the C-terminal peptide bonds of arginine (R) and lysine (K), while Lys-C specifically cleaves the C-terminal peptide bonds of lysine (K). This combination overcomes issues such as the slower digestion rate of lysine and arginine by rTrypsin, PTM changes on lysine, or hydrophobic C-termini (such as proline) that can lead to missed cleavage. Trypsin/Lys-C complex protease (MS grade) can be used to process complex protein samples that are difficult to enzymatically digest. Trypsin/Lys-C complex protease (MS grade) can be used for protein characterization, single-cell proteomics and large cohort proteomics studies.

Nitrilase is able to hydrolyze nitriles into their corresponding carboxylic acids and ammonia. Nitrilase is a green biocatalyst for the production of high value-added products.

Kallikrein, Porcine pancreas (kininogenase) is capable of forming the kallikrenase kalinin system (KKS) in plasma and tissues, producing bradykinin and kalin peptides, respectively.

IgdE protease is a cysteine protease, which is initially isolated from Streptococcus agalactiae. IgdE protease digests monoclonal antibodies (mAbs) of the IgG1 type specifically at their upper hinge region, produces Fc/2, hinge peptide dimers, and Fab fragment. IgdE protease can be used in disulfide bonds and free thiol analysis, as it requires no reducing agents for cleavage.

Cathepsin G is a pH-dependent serine protease. Cathepsin G hydrolyzes diverse synthetic and protein substrates and remodels extracellular matrix. Cathepsin G exerts immunomodulatory effects via recruiting phagocytes, enhancing T cell motility, activating ERK1/2 and p38 MAPK signaling, and mediating PKCζ membrane translocation. Cathepsin G regulates inflammatory responses by cleaving inflammatory mediators. Cathepsin G participates in vascular regulation by converting angiotensin I to angiotensin II. Cathepsin G induces PAR4-dependent platelet activation, facilitates platelet-neutrophil aggregation, and mediates VITT-related NETosis, thrombus formation. Cathepsin G can be used for the research of immune thrombotic thrombocytopenia, cardiovascular disease, and select autoimmune and inflammatory diseases.

Enteropeptidase (TMPRSS15), a type II transmembrane serine protease and a physiological activator of trypsinogen. Enteropeptidase is associated with the brush border membrane (BBM) of the enterocytes in the upper small intestine. Trypsinogen is the primary substrate for Enteropeptidase. Enteropeptidase is involved in digestion in humans and animals.

Cre recombinase is a resolvase derived from the P1 bacteriophage. Cre recombinase catalyzes site-specific recombination between two loxP DNA sequences, converts dimers of P1 chromosome into monomers before cell division. Cre recombinase is utilized in genetic engineering and molecular biology applications.

Keratanase II,bacillus circulans,expressed in E.coli has transglycosylation activity. Keratanase II,bacillus circulans,expressed in E.coli efficiently catalyzes the transglycosylation of α(2→3)-sialylated 6,6′-di-sulfo-LacNAc with two kinds of glycosyl acceptors, 6-sulfo-Lewis X and 6,6'-di-sulfo-LacNAc derivatives, providing Sialyl sulfo-hexasaccharide and Sialyl sulfo-pentasaccharide.

Phospholipase C (PLCs) is a class of phospholipases. Phospholipase C participates in cellular signaling and regulation by virtue of its ability to hydrolyze membrane phospholipids into di-acyl-glycerol (DAG) and inositol triphosphate (IP3), which further causes the activation of other signaling pathways involved in various processes, including immune response.

Carboxypeptidase A, Bovine pancreas (EC 3.4.2.1) is a zinc-containing metalloprotease, is often used in biochemical studies. Carboxypeptidase A catalyzes the hydrolysis of the peptide bonds that are adjacent to the C-terminal end of a polypeptide chain. Carboxypeptidase A is a prototypical enzyme for metalloproteases that plays important roles in biological systems.

Polynucleotide Kinase is a DNA repair enzyme. Polynucleotide Kinase possesses both a 5’-kinase activity that catalyzes the transfer of phosphate from ATP to a 5’-hydroxyl (OH) terminus and also a 3’-phosphatase activity that converts 3’-phosphate termini to 3’-OH termini.