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Native Aspergillus niger Cellobiase Purified 1

 

Cellobiase enzyme preparation obtained by submerged fermentation of an Aspergillus niger microorganism. The cellobiase hydrolyzes cellobiose to glucose.

Cellobiase enzyme preparation obtained by submerged fermentation of an Aspergillus niger microorganism. The cellobiase hydrolyzes cellobiose to glucose.

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Native Baker's yeast (S. cerevisiae) Carboxypeptidase Y LAB GRADE 1

 

Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by diisopropyl fluorophosphate.

Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by diisopropyl fluorophosphate.

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Native Bovine Protamine Kinase, Cytosolic LAB GRADE 1

 

Cytosolic protamine kinase is involved in the regulation of protein synthesis and is indirectly associated with numerous cellular processes. Cytosolic protamine kinase is a distinct insulin-stimulated kinase involved in the phosphorylation of eukaryotic Initiation Factor 4E (eIF4E) which is key to initiating translation by mRNA. This protein appears to be inactivated by protein phosphatase 2A family members and may also be inhibited by microcystin, okadeic acid, and ATP. The phosphorylation process is reversible and MBPK1 and MBPK2 (Myelin Basic Protein Kinase 1 and 2) may reactivate cytosolic protamine kinase.

Cytosolic protamine kinase is involved in the regulation of protein synthesis and is indirectly associated with numerous cellular processes. Cytosolic protamine kinase is a distinct insulin-stimulated kinase involved in the phosphorylation of eukaryotic Initiation Factor 4E (eIF4E) which is key to initiating translation by mRNA. This protein appears to be inactivated by protein phosphatase 2A family members and may also be inhibited by microcystin, okadeic acid, and ATP. The phosphorylation process is reversible and MBPK1 and MBPK2 (Myelin Basic Protein Kinase 1 and 2) may reactivate cytosolic protamine kinase.

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Native Lignin Peroxidase from Phanerochaete chrysosporium LAB GRADE 1

Lignin peroxidase is a fungal enzyme which has a key role in the ligninolytic cycle, the process by which the structural component of plant walls, lignin, is degraded.

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Native Microorganism Glucose Dehydrogenase (FAD-dependent) LAB GRADE 1

 

FAD-GDH catalyses the oxidation of glucose in the presence of an electron acceptor, such as 2,6-dichlorophenolindophenol or potassium ferricyanide.

FAD-GDH catalyses the oxidation of glucose in the presence of an electron acceptor, such as 2,6-dichlorophenolindophenol or potassium ferricyanide.

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Native Porcine Colipase LAB GRADE 1

 

Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. In humans, the colipase protein is encoded by the CLPS gene.

Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. In humans, the colipase protein is encoded by the CLPS gene.

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Native Porcine L-Lactate Dehydrogenase LAB GRADE 1

A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.

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Native Spinacia oleracea (Spinach) Ferredoxin-NADP+ Reductase LAB GRADE 1

 

Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria.

Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria.

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PVPP FOOD GRADE FOOD GRADE 94%MIN

Chemical description:

--Polyvinylpolypyrrolidone, Cross - linked PVP

Characteristics:

--A white to creamy white powder;

--Practically insoluble in water, alcohol, methylene chloride

Application:

--Good filtration auxiliary in the clarification of beer, wine and fruit juice.

Packaging and store:

--Packaged in 20kg fibre or plastic drum, inner lined with PE bags;

--Stored in a dry place at room temperature.

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