- Enzymes
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DNase I (EC 3.1.21.1) is an enzyme that degrade DNA, it plays a key role in the cleavage of extracellular DNA is crucial for limiting the inflammatory response and maintaining homeostasis. Exogenous deoxyribonuclease shows beneficial effects in inflammatory diseases and cancer.
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- Masse moléculaire: 68-130 kDa
Collagenase, Type IV (EC 3.4.24.3) is a microbially derived matrix metalloproteinases (MMPs) and zinc peptidase. Collagenase, Type IV degrades type IV collagen and type VII collagen, the main components of the basement membrane, and can also decompose basement matrix and elastin.
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- Masse moléculaire: 68-130 kDa
Collagenase, Type II is a microbially derived matrix metalloproteinases (MMPs) and zinc peptidase. Collagenase, Type II breaksdown collagens1, 3, 5, 7, 8, 10, fibronectin, gelatin, aggrecann.
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- Formule: C1135H1759N331O346S10
- Masse moléculaire: 25898.13
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- Masse moléculaire: 68-130 kDa
Collagenase, Type I is a microbially derived matrix metalloproteinases (MMPs) and zinc peptidase. Collagenase, Type I breaks down collagens 1, 3, 7, 8, 10, gelatin, proteoglycans, aggrecan.
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Cholesterol oxidase, Microorganism (ChOx) is a cholesterol oxidase identified from bacterial sources. Cholesterol oxidase, Microorganism catalyzes the oxidation of cholesterol to 4-cholesten-3-one, while simultaneously reducing oxygen to hydrogen peroxide. Cholesterol oxidase, Microorganism retains its enzymatic activity and exhibits improved catalytic efficiency upon immobilization. Cholesterol oxidase, Microorganism is applicable for cholesterol detection, steroid biotransformation, and research on tuberculosis-related diseases.
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Endo-1,3-β-glucanase (Lyticase) is an endoenzyme that can specifically cleave β-1,3-glycosidic bonds. Endo-1,3-β-glucanase recognizes and binds to β-1,3-glucan chains, catalyzing the cleavage of glycosidic bonds and hydrolyzing polysaccharides into oligosaccharides. Endo-1,3-β-glucanase eliminates vaginal Candida. Endo-1,3-β-glucanase can be used in the study of recurrent Candida vaginitis.
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Endo-1,4-β-mannanase is an important catalyst that randomly cleaves the β-1,4-linkages in the main chain of mannan, releasing short-chain β-1,4-mannan and mannose. The catalytic activity of Endo-1,4-β-mannanase toward locust bean gum is enhanced by Mn2+, Co2+, Ca2+, Ba2+, Triton X-100, sodium azide and N-ethylmaleimide, completely inhibited by Hg2+ and N-bromosuccinimide, and partially inhibited by EDTA and Cu2+. Endo-1,4-β-mannanase can be used in studies related to plant hemicellulose degradation, biomass saccharification, elimination of anti-nutritional factors in feed, and manno-oligosaccharide prebiotics.
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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.
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- Masse moléculaire: 34000 (monomer)
L-Asparaginase (L-ASNase) is a deamidating enzyme that catalyses the hydrolysis of L-asparagine and L-glutamine, and can be used for the research of acute lymphoblastic leukemia. L-Asparaginase depletes L-asparagine from plasma resulting in inhibition of RNA and DNA synthesis with the subsequent blastic cell apoptosis.
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Tyrosinase (EC 1.14.18.1) (Polyphenol oxidase) is a rate-limiting enzyme that controls the production of melanin. Tyrosinase is mainly found in melanosomes synthesized by skin melanocytes. Tyrosinase can be used in research on Parkinson's disease, melanoma and pigmentation.
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Apyrase is an Nucleoside triphosphate diphosphohydrolase (NTPDase). Apyrase can hydrolyze extracellular adenosine triphosphate (ATP) and adenosine diphosphate (ADP). Apyrase can inhibit Stx2 toxin release of enterohemorrhagic Escherichia coli (EHEC) infection and protect the intestinal barrier function. Apyrase can be used for the research of infection and inflammation, such as hemorrhagic colitis.
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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.
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Transglutaminase, Streptoverticillium mobaraense (TG) is an enzyme that forms cross-links between protein molecules. Transglutaminase, Streptoverticillium mobaraense attaches proteins and peptides to small molecules, polymers, surfaces, DNA and other proteins. Transglutaminase, Streptoverticillium mobaraense is widely used in food applications in the meat, fish, dairy and baking industries.
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RNase A (Bovine pancreatic RNase) is a widely used Endonuclease in DNA purification by specifically hydrolyzing cytosine or uracil residues of RNA. RNase A degrades the RNA in the RNA/DNA duplex. RNase A catalyses the breakdown of 3',5'-phosphodiester linkages of single stranded RNA. RNase A family members in organisms are tightly involved in various physiological and pathological processes including cell growth and development, proliferation, differentiation and migration. Dysregulation of RNase A activity or expression level is closely related to pancreatic, ovarian, bladder and thyroid cancer. RNase A has tumor cell-killing ability.
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Peroxidase, Horseradish actively involves in oxidizing reactive oxygen species, innate immunity, hormone biosynthesis and pathogenesis of several diseases.
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Catalase, Aspergillus niger is a key enzyme in the metabolism of H2O2 and reactive oxygen species (ROS), and its expression and localization is markedly altered in tumors. Free oxygen radical scavenger.
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