Protease

Endoproteinase Asp-N (MS grade) is a metalloprotease that can specifically cleave the N-terminal side of aspartyl and cysteic acid residues.

Mucinase StcE is a zinc metalloproteinase belonging to the M66 family, which is secreted by enterohemorrhagic Escherichia coli via the type II general secretion pathway. Mucinase StcE specifically recognizes and cleaves the 'T*XT' motif in mucin-type glycoproteins with α-O-glycans (such as MUC2, Mucin 7, Glycoprotein 340, CD45, CD43, C1 Esterase Inhibitor (HY-P991629), etc.). By degrading the mucus layer to reduce its viscosity, inhibiting complement cascade activation, and localizing complement regulatory factors to the cell membrane, Mucinase StcE helps bacteria penetrate the mucosal barrier, adhere to host cells, and evade immune clearance. Mucinase StcE can serve as a mucin-specific proteolytic tool for research on mucinous carcinomas derived from the colon, esophagus, and salivary glands.

Proteinase K (Protease K) (NGS grade) is a nonspecific serine protease that is useful for general digestion of proteins. Proteinase K (NGS grade) is active in the presence of SDS or urea and over a wide range of pH (4-12), salt concentrations, and temperatures. Proteinase K (NGS grade) can be use for promoting methods of viral nucleic acid extraction, and detection. This product is NGS grade, no Nickase residue, and nucleic acid residue ≤5 pg/mg.

Dextranase, Trichoderma reesei belongs to glycoside hydrolase family 49. It catalyzes the hydrolysis of α-1,6-glycosidic linkages in dextran via a single-displacement reaction, ultimately releasing shorter isomaltooligosaccharides. Dextranase, Trichoderma reesei reduces the molecular size of dextran, inhibits the formation of insoluble dextran and dental plaque, and decreases the viscosity of dextran-contaminated sugar juice. Dextranase, Trichoderma reesei can be used in relevant research in fields such as chemical production, including beer manufacturing, feed additives, and toothpaste formulations.

Triacylglycerol lipase is an enzyme catalyzing the hydrolysis of triacylglycerol. Triacylglycerol lipase promotes fat decomposition, providing energy and lipid precursors for cells. Triacylglycerol lipase is used in the research of metabolic diseases such as diabetes and obesity.

Alginate lyase is a polysaccharide lyase that catalyzes the degradation of alginate. Alginate lyase can be used for the research of cystic fibrosis by degrading the polysaccharide biofilm of Pseudomonas aeruginosa.

Proteinase, Aspergillus oryzae is a serine protease that hydrolyzes peptide bonds in protein substrates, preferring alkaline conditions (optimal pH 10.5). It efficiently degrades casein, poly-L-glutamic acid, and poly-L-lysine, with activity irreversibly inhibited by diisopropylfluorophosphate (DFP) and potato inhibitor. This enzyme catalyzes proteolysis via serine residues in its active site, finding applications in food processing (e.g., soy sauce fermentation), detergents, and leather industries due to its high yield in solid-state fermentation and cost-effective production.

Lipoprotein lipase, Pseudomonas sp (LPL) is a multifunctional enzyme from adipose tissue, heart and skeletal muscle, islets and macrophages. Lipoprotein lipase promotes normal lipoprotein metabolism, delivery and utilization of tissue-specific substrates. Lipoprotein lipase catalyzes the rate-limiting step of lipids in blood circulation.

Carboxypeptidase B, Porcine pancreas (EC 3.4.2.2) is a peptide exonuclease that can specifically degrade peptide chains. Carboxypeptidase B is progressively degraded from the C-terminal to release free amino acids. Carboxypeptidase B hydrolyzes only peptide bonds with basic amino acids (such as arginine and lysine) as C-terminal residues.

Endoproteinase Lys-C (MS grade) is a hydrolase that cleaves peptide bonds at the carboxyl side of lysine residues. Endoproteinase Lys-C (MS grade) causes non-specific hydrolysis of peptide bonds linked to the carboxyl groups of non-lysine residues, resulting in partial cleavage at these sites.

HRV-3C protease fuses with GST is a recombinant protease fused with HRV-3C protease and GST, which recognizes the LEVLFQGP polypeptide sequence. HRV-3C protease fuses with GST precisely cleaves between glutamine and glycine-proline residues to remove fusion tags from target proteins. HRV-3C protease fuses with GST exhibits cleavage activity both in vitro in silkworm fat body lysates and in vivo in silkworm larval fat bodies, and achieves functional expression in E. coli and silkworm-baculovirus expression systems. HRV-3C protease fuses with GST can be applied to recombinant protein-related research.

SUMO Protease is highly specific for proteins containing small ubiquitin-like modifier (SUMO) tags. SUMO Protease can be used to regulates the proteins splicing, controlls protein structure and function in vitro.

Recombinant Proteinase K (Protease K) (DNase & RNase free, animal free) is a nonspecific serine protease that is useful for general digestion of proteins. Proteinase K (DNase & RNase free, animal free) is active in the presence of SDS or urea and over a wide range of pH (4-12), salt concentrations, and temperatures. Proteinase K (DNase & RNase free, animal free) can be use for promoting methods of viral nucleic acid extraction, and detection. This product is of molecular biology grade, free of animal-derived ingredients, and is recombinantly purified from yeast.

Chitinase, Serratia marcescens is a chitinase from Serratia marcescens. 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.

Stem bromelain (EC 3.4.22.32) is a cysteine protease and antibacterial agent. Stem bromelain can be isolated from the stem of the pineapple (Ananas comosus). Stem bromelain induces dose-dependent secretion of IL-12p70, and IL-6, induces Apoptosis, causes cleavage of full-length PARP protein, Caspase 3, and Caspase 9, increases Bax, and decreases Bcl-2. Stem bromelain possesses various fibrinolytic, antiedema, antithrombotic, and anti-inflammatory activities. Stem bromelain also exhibits in vivo antitumor and antileukemic activities, as well as antimetastatic effects. Stem bromelain has antimycobacterial activity. Stem bromelain provides protection against lead poisoning.

Lysyl endopeptidase, Achromobacter sp (Lys-C) catalyzes carboxyl oxygen exchange reaction. Lysyl endopeptidase has higher substrate binding affinities and higher catalytic rates at the acidic pHs than at the alkaline pHs.

Ficain is an enzyme extract composed of several proteases that can be isolated from Ficus hispida L. and the latex of fig (Ficus carica). Ficain has different specificities in different proportions during fruit ripening. Ficain is widely used in protein hydrolysis, food, production of bioactive peptides and antibody fragments.

Pullulanase (R-enzyme) is a key starch debranching enzyme that specifically hydrolyzes α-1,6-glycosidic linkages in polysaccharides such as amylopectin and pullulan, facilitating the efficient degradation of starch into fermentable sugars.

Rennin, also known as Chymosin, is a pepsin-related proteolytic enzyme synthesized by cells in the stomach of certain animals that efficiently converts liquid milk into a semi-solid, allowing it to remain in the stomach for longer. The natural substrate of Rennin is K-casein, which is specifically cleaved at the peptide bond between amino acid residues 105 and 106, phenylalanine and methionine, and is widely used in cheese production.

Streptokinase, β-hemolytic streptococcus (Lancefield Group C) is a bacteria-derived protein and a plasminogen activator. Streptokinase is widely used for the research of the blood-clotting disorders. Streptokinase improves reperfusion blood flow after coronary artery occlusion.