
Enzymes dans les Protéines Recombinantes
3320 produits trouvés pour "Enzymes dans les Protéines Recombinantes"
Cocarboxylase hydrochloride
CAS :Cocarboxylase hydrochloride is a coenzyme derivative, which is primarily sourced from thiamine (vitamin B1). It plays a crucial role in biochemical processes by facilitating the enzymatic decarboxylation of alpha-keto acids within the cellular environment. This action is fundamental in energy production as it aids in the conversion of pyruvate to acetyl-CoA, subsequently entering the citric acid cycle. Cocarboxylase hydrochloride’s involvement in carbohydrate metabolism is especially vital for tissues with high metabolic rates, such as the heart and brain.
Formule :C12H19N4O7P2S·ClHClDegré de pureté :Min. 95%Masse moléculaire :497.23 g/molAcetylcholinesterase, type VI-S, 200-1,000 units/mg protein
CAS :Acetylcholinesterase is an enzyme that breaks down acetylcholineDegré de pureté :Min. 95%Couleur et forme :PowderTransglutaminase from streptoverticillium mobaraense
CAS :selectively deamidates gluten peptides, which results in strongly enhanced T cell-stimulatory activity. It has also been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.Couleur et forme :PowderButyrylcholinesterase human
CAS :Butyrylcholinesterase is an enzyme made in the liver and found mainly in blood plasma. Butyrylcholinesterase (EC 3.1.1.8), also known as BChE or BuChE, is a nonspecific cholinesterase enzyme that hydrolyses choline-based esters. One unit of Butyrylcholinesterase will hydrolyze 1.0 μmole of butyrylcholine to choline and butyrate per minute at pH 8.0 and 37 °C.
Couleur et forme :PowderProteinase K - from Tritirachium album
CAS :Proteinase K is used for the general digestion of proteins and removal of protein contamination in nucleic acids. Addition of Protease K also stabilizes nucleic acids by degrading any nucleases present. Proteinase K is active in wide range of pH range, in the presence of SDS, urea and Guanidinium chloride at low to moderate concentrations. Proteinase K is also known under names of protease K and endopeptidase K.β-Galactosidase >100KU/g
CAS :beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated.Couleur et forme :PowderNucleoside phosphorylase from microorganisms
CAS :Nucleoside phosphorylase (Purine nucleoside phosphorylase, PNP, PNPase, inosine phosphorylase, inosine-guanosine phosphorylase; EC 2.4.2.1) is an enzyme that catalyzes the following reaction: purine nucleoside + Pi ⇌ purine + alpha-D-ribose 1-phosphate One unit of nucleoside phosphorylase will phosphorylate 1.0 micromole of inosine to hypoxanthine and alpha-D-ribose 1-phosphate per min at pH 7.4 and 25°C.Formule :C5H6ClN3Degré de pureté :Min. 95%Masse moléculaire :143.57 g/molCarboxypeptidase Y from baker's yeast
CAS :Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product.Degré de pureté :Min. 95%Glyceraldehyde-3-phosphate dehydrogenase
CAS :75u/mg - Glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) is an enzyme that catalyzes the following reaction: glyceraldehyde 3-phosphate + NAD+ + Pi ⇌ glycerate 1,3-bisphosphate + NADH + H+ One unit of GAPDH will convert 1.0 μmole of glyceraldehyde 3-phosphate into glycerate 1,3-bisphosphate per minute at pH 8.5 and 37 °C in the presence of NAD+ and phosphate. NAD+ is available here.Formule :C3H7O6PDegré de pureté :Min. 95%Masse moléculaire :170.06 g/molLysozyme - Enzyme activity min 40000 FIP/mg
CAS :Lysozyme is a bacteriolytic enzyme, which is primarily derived from hen egg whites. It functions by hydrolyzing the β-1,4-glycosidic linkages in the peptidoglycan layer of bacterial cell walls, particularly in Gram-positive bacteria. This enzymatic activity results in the lysis and subsequent death of the bacterial cells, providing a potent antimicrobial effect.Couleur et forme :PowderSulfatase, from helix pomatia ≥10,000 units/g solid
CAS :Sulfatase from Helix pomatia is a highly potent enzyme that is capable of hydrolyzing sulfated compounds and sulfate esters. It has been widely used in various applications such as glucosinolate analysis, genistein extraction preparation, and regiospecificity studies. With a concentration of ≥10,000 units per gram of solid, this sulfatase offers exceptional enzymatic activity for sulfatase assays. It effectively catalyzes the hydrolysis of sulfated substrates, including p-nitrocatechol sulfate, naphthyl sulfate and phenyl sulfates.The enzyme can be incubated with the desired sample to facilitate the release of sulfate groups from sulfated compounds. Sulfatase from Helix pomatia is a valuable tool for researchers and scientists working in diverse fields requiring efficient and reliable enzymatic hydrolysis capabilities. Additionally the enzyme has been found to have industrial applications, such as in the bioconversion of industrial chemicals, where it can be used as a catalyst.
Couleur et forme :PowderThioredoxin reductase from escherichia coli
CAS :Thioredoxin reductase (TR, TrxR) (EC 1.8.1.9) is an enzyme that reduce thioredoxin using NADPH as a co-factor, and also contains FAD. One unit of thioredoxin reductase will raise increase light absorbance by 1.0 per minute at 412nm in the presence of thioredoxin and Ellman's reagent at pH 7.0 and 25 °C.Degré de pureté :Min. 95%Glycerol 3-phosphate oxidase, from pediococcus sp., 40-84U/mg
CAS :Glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the following reaction: glycerol-3-phosphate + O2 ⇌ dihydroxyacetone phosphate + H2O2 One unit of Glycerol-3-phosphate oxidase will generate 1.0 μmole H2O2 per min at 37°C, under the presence of O2 and the optimal pH. If required, you can remove the build-up of hydrogen peroxide using catalase.Degré de pureté :Min. 95%Glycerokinase, cellulomonas species
CAS :Glycerokinase (glycerol kinase, GP, ATP-glycerol 3-phosphotransferase; EC 2.7.1.30) is an enzyme that catalyzes the following reaction: ATP + glycerol ⇌ ADP + glycerol 3-phosphate One unit of Glycerokinase will convert 1.0 μmole of glycerol and ATP to glycerol 3-phosphate and ADP per min at pH 9.8 and 25 °C.Couleur et forme :PowderTriose phosphate isomerase
CAS :Triose-phosphate isomerase (TPI, TIM; EC 5.3.1.1) is an enzyme that catalyzes the reversible isomerisation of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate: DHAP ⇌ GADP The reaction mechanism involves the formation of an enediol intermediate. One unit of Triose-phosphate isomerase will convert 1.0 μmole glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 and 25 °C.Degré de pureté :Min. 95%Oxalate Oxidase, freeze-dried, from Wheat
CAS :Oxalate Oxidase, freeze-dried, is an enzymatic preparation that serves as a catalyst in biochemical reactions. This enzyme is derived from wheat, a common plant source, ensuring a naturally occurring origin. Its primary mode of action is the oxidation of oxalate into carbon dioxide and hydrogen peroxide. This biochemical activity is significant in various scientific applications, specifically in the breakdown of oxalate, which plays a crucial role in metabolic and environmental processes.Couleur et forme :Powderβ-Glucuronidase from Helix pomatia - Type H-2, aqueous solution, ≥85,000 units/mL
CAS :β-Glucuronidase (EC 3.2.1.31) is an enzyme that hydrolyzes glucuronides. It can also be used to cleave benzodiazepine and steroid conjugates. One unit of β-Glucuronidase will hydrolyze a chromogenic substrate mimic 4-nitrophenyl-β-D-glucuronide to produce 1.0 μmole of 4-nitrophenol per minute at pH 5.0 and 37 °C.Degré de pureté :Min. 95%Couleur et forme :Clear LiquidSarcosine oxidase from bacillus sp., >15 units/mg solid, lyophilized powder
CAS :Sarcosine oxidase (Monomeric sarcosine oxidase, MSOX, EC 1.5.3.1) is an enzyme that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2 and formaldehyde in the following reaction: CH3-NH2+-CH2-COO- + H2O + O2 → NH3+-CH2-COO- + H2O2 + CH2O or sarcosine + water + oxygen → glycine + hydrogen peroxyde + formaldehydeOne unit of Sarcosine oxidase will form 1.0 micromole of formaldehyde from sarcosine per minute at pH 8.3 and 37 °C. You can remove the build-up of hydrogen peroxide using catalase.Formule :C10H12N8O3Degré de pureté :Min. 95%Couleur et forme :PowderMasse moléculaire :292.25 g/molAlkaline phosphatase
CAS :One unit of alkaline phosphatase (EC 3.1.3.1) will hydrolyze 1.0 µmol of 4-nitrophenyl phosphate per min at 25°C and pH 9.6.Degré de pureté :Min. 95%Couleur et forme :PowderKRAS Protein, Human, Recombinant (G12S, GST)
Expression system: E. coli<br>Length: 1-169, Partial<br>Activity: BLI
Couleur et forme :Odour Lyophilized Powder

