Protease

Elastase, Porcine pancreas (EC 3.4.21.36) is a single polypeptide chain of 240 amino acid residues, derived from pig pancreas. Elastase, Porcine pancreas is a serine protease that can hydrolyze proteins and polypeptide. Elastase from porcine pancreas can induce emphysema in hamsters.

Pepsin is the major pig and human gastric proteases, it is a pepsin-like minor gastric proteolytic enzymes. Pepsin contributes to proteolysis of food proteins in the vertebrate stomach.

TPCK-treated Trypsin is a trypsin whose activity is inhibited by tosyl phenylalanyl chloromethyl ketone. TPCK-treated Trypsin reduces autolysis and nonspecific proteolysis during experiments, exhibits stability in storage and handling. TPCK-treated trypsin can be used in proteomics research. TPCK-treated Trypsin renders the virus hemagglutinin active, which allows multicycle replication of the virus. TPCK-treated Trypsin can be used for the study of influenza virus.

Chymotrypsin (EC 3.4.21.1; Chymotrypsin A) is an orally effective inhibitor targeting molecules such as TLR4, NF-κB, MMP-1, TNF-α, IL-1β, and IL-6. Chymotrypsin downregulates the TLR4/NF-κB signaling pathway, inhibiting the release of inflammatory factors, reducing cell infiltration and tissue damage. It also reduces the expression of tumor cell adhesion molecules (such as CD44 and CD54) and can be specifically detected by fluorescent probes (such as NBD-3). Chymotrypsin has anti-inflammatory, hepatoprotective, joint damage-reducing, liver protection against lipotoxicity, and anti-tumor metastasis functions. It can be used in research on diseases such as rheumatoid arthritis, non-alcoholic fatty liver disease, and melanoma metastasis. Chymotrypsin can be used in studies of inflammation, edema, and expectoration.

Thermolysin, Bacillus thermoproteolyticus rokko (EC 3.4.24.27) (TML) is a thermostable neutral metalloproteinase enzyme secreted by the Gram-positive bacteria Bacillus thermoproteolyticus. Thermolysin catalyzes the hydrolysis of peptide bonds containing hydrophobic residues.

Optimal pH: 8.0. Considerably stable from pH 5 to 9.5.
Optimal temperature : 70 °C

γ-D-Glutamyl-meso-diaminopimelate peptidase (EC 3.4.19.11) is a 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family) . Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism.

Endoproteinase Lys-C is a protease that cleaves proteins on the C-terminal side of lysine residues and is commonly used for protein sequencing.

Trypsin MS grade is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin MS grade activates PAR2 and PAR4. Trypsin MS grade induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin MS grade also promotes cell proliferation and differentiation. Trypsin MS grade can be used in the research of wound healing and neurogenic inflammation.

Endoproteinase Lys-C (Tag-free) is a protease that cleaves proteins on the C-terminal side of lysine residues and is commonly used for protein sequencing.

Subtilisin (Compound proteinase) (EC 3.4.21.62) is a proteolytic enzyme, isolated from Bacillus licheniformis. Subtilisin (Compound proteinase) has catalytic activity in anhydrous dimethyl formamide. Subtilisin (Compound proteinase) can be used as a catalyst for easy coupling between sugars and amino acids.

Endoproteinase Lys-N (MS grade) is a protease that specifically hydrolyzes the N-terminal peptide bond of lysine fragments.

hrv 3c Protease is a protease originated from human rhinoviruses. hrv 3c Protease recognizes the sequence LEVLFQGP and cleaves precisely between the Q and GP residues. hrv 3c Protease can be used to remove additional tags from the target proteins.

Heparitin sulfate lyase (Heparinase III) is a glycosidic lyase targeting heparan sulfate and heparin. Heparitin sulfate lyase is promising for research of low-molecular-weight heparin production and cancers.

Chitinase, Streptomyces griseus is a chitinase from Streptomyces griseus. 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.

Subtilisin (EC 3.4.21.14) is a bacterial serine protease. Subtilisin induces Apoptosis. Subtilisin stimulates the expression of pro-allergic cytokines (IL-1α, IL-33). Subtilisin induces prototypic allergic lung inflammation. Subtilisin exhibits anticancer activity against breast and colon cancer. Subtilisin shows antifouling activity. Subtilisin can be used as a detergent additive.

Microbial neutral proteinase is a zinc-containing metalloproteinase mainly produced by Bacillus and fungi. Its catalytic activity is highly dependent on divalent cations, and it remains active within the pH range of 5-8. Microbial neutral proteinase can specifically cleave peptide bonds within polypeptide chains, thereby degrading macromolecular proteins into small peptides or amino acids. It can be applied in various industrial fields including food processing, brewing, detergents, and light industry.

Recombinant enterokinase (rEK) is a serine protease and functions as the physiological activator of trypsinogen. Recombinant enterokinase plays a role of turning trypsinogen to its active form trypsin.

TLCK-treated Chymotrypsin is a serine protease. Chymotrypsin cleaves protein chains at the carboxyl side of aromatic amino acids. TLCK treated to inactivate residual tryspin activity.