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Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!2025-02-06
345 Results for "
paracolon bacillus
" in MedChemExpress (MCE) Product Catalog:
Products (345)
345 Results for "paracolon bacillus" in MCE Product Catalog:
Cat. No.: HY-P2859B
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Chitosanase, Bacillus sp (EC 3.2.1.132) is a chitosanase preparation produced by deep fermentation of Bacillus strains. Chitosanase, Bacillus sp (EC 3.2.1.132) catalyzes the decomposition of chitosan.
Cat. No.: HY-E70913A
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Phosphotransacetylase, Bacillus stearothermophilus (EC 2.3.1.8) converts coenzyme A to acetyl-CoA. Phosphotransacetylase, Bacillus stearothermophilus (EC 2.3.1.8) belongs to the transtransferase family and participates in three metabolic pathways: taurine and linolenic acid metabolism, pyruvate metabolism, and propionic acid metabolism.
Cat. No.: HY-E70940B
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Sphingomyelinase, Bacillus cereus (EC 3.1.4.12) is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. Sphingomyelinase, Bacillus cereus (EC 3.1.4.12) is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide.
Cat. No.: HY-E70903
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Thermitase, Bacillus cereus is a protease that inactivates Rnases, Dnases and enzymes in reactions.
Cat. No.: HY-P2817B
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Phospholipase C, Bacillus cereus (EC 3.1.4.3) is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid. Phospholipase C, Bacillus cereus (EC 3.1.4.3) hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol. Phospholipase C, Bacillus cereus (EC 3.1.4.3) hydrolyzes the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids.
Cat. No.: HY-E70124I
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Esterase, Bacillus thermoglucosidasius (EC 3.1.1.1) is a hydrolase that splits esters into acids and alcohols
Cat. No.: HY-P2952B
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Myokinase, Bacillus stearothermophilus (EC 2.7.4.3) for research on ATP metabolism and enzymatic mechanisms.
Cat. No.: HY-P2806B
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Pyruvate Kinase, Bacillus stearothermophilus (EC 2.7.1.40) is an enzyme involved in glycolysis. Pyruvate Kinase, Bacillus stearothermophilus (EC 2.7.1.40) catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP.
Cat. No.: HY-E70981
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Alanine Racemase, Bacillus stearothermophilus (EC 5.1.1.1) is involved in alanine, aspartate and D-alanine metabolism. Alanine Racemase, Bacillus stearothermophilus (EC 5.1.1.1) monomer is composed of two domains, an eight-stranded α/β barrel at the N-terminus and a C-terminal domain.
Cat. No.: HY-P3000A
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Myo-Inositol Dehydrogenase, Bacillus subtilis (EC 1.1.1.18) is an oxidoreductase that acts on the donor CH-OH group and uses NAD+ or NADP+ as the acceptor. Myo-Inositol Dehydrogenase, Bacillus subtilis (EC 1.1.1.18) is involved in inositol metabolism and inositol phosphate metabolism.
Cat. No.: HY-P2992A
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Inorganic Pyrophosphatase, Bacillus stearothermophilus (EC 3.6.1.1) catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. The functionality of Inorganic Pyrophosphatase, Bacillus stearothermophilus (EC 3.6.1.1) plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations.
Cat. No.: HY-E71001
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L-Leucine Dehydrogenase, Bacillus cereus (EC 1.4.1.9) is a redox enzyme that acts on the donor CH-NH2 group and uses NAD+ or NADP+ as the acceptor. L-Leucine Dehydrogenase, Bacillus cereus (EC 1.4.1.9) participates in the degradation of valine, leucine, and isoleucine, as well as their biosynthesis.
Cat. No.: HY-E70994
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Fructose-6-phosphate Kinase, Bacillus stearothermophilus (EC 2.7.1.11) is an important enzyme in glucose metabolism. Fructose-6-phosphate Kinase, Bacillus stearothermophilus (EC 2.7.1.11) catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate.
Cat. No.: HY-E70103H
CAS No.: 9067-74-7
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exo-α-Arabinofuranosidase, Bacillus subtilis (EC.3.2.1.55) is a glycoside hydrolase .
Cat. No.: HY-P2993E
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Isocitrate dehydrogenase, Bacillus subtilis (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2.
Cat. No.: HY-P2854A
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L-Alanine Dehydrogenase, Bacillus subtilis (EC 1.4.1.1) is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium.
Cat. No.: HY-E70913
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Phosphotransacetylase, Bacillus subtilis (EC 2.3.1.8), converts coenzyme A to acetyl-CoA. Phosphotransacetylase is an acyltransferase that transfers groups other than aminoacyl groups. Phosphotransacetylase participates in three metabolic pathways: taurine and hypoturine metabolism, pyruvate metabolism, and propionic acid metabolism.
Cat. No.: HY-E70936A
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Glycerokinase, Bacillus stearothermophilus (EC 2.7.1.30) is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerokinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol.
Cat. No.: HY-P2768A
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Leucine dehydrogenase, Bacillus sp. (EC 1.4.1.9) is a carboxyl lyase that cleaves carbon-carbon bonds. L-Arginine Decarboxylase has one substrate, L-arginine, and two products, guanidine and CO2.
Cat. No.: HY-P2918E
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Phosphoglucose isomerase, Bacillus subtilis (EC 5.3.1.9) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. Phosphoglucose isomerase is responsible for the second step of glycolysis and is involved in glucogenesis.
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Protocols
Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!A suitable model is crucial in drug screening experiments. Organs can mimic the three-dimensional functional structure of internal organs, have similar spatial organization to corresponding organs, maintain some key characteristics, and reproduce some physiological functions. They are widely used for modeling and personalized drug screening physiological functions.2025-02-06
