
Enzima
Sottocategorie di "Enzima"
- Anidrasi carbonica(196 prodotti)
- Idrossilasi(36 prodotti)
- MPO(2 prodotti)
- Riduttasi(51 prodotti)
- Tirosinasi(71 prodotti)
Trovati 3619 prodotti di "Enzima"
Cathepsin B from human placenta
CAS:Cathepsin B is a lysosomal proteolytic enzyme of the cysteine protease family. It is present in all mammalian cells. It is essential for the intracellular protein turnover. Cathepsin B may be a useful tool in Alzheimer′s research, as it may have a role in the natural defense against the disease.Purezza:Min. 95%Carboxypeptidase Y, from S. cerevisiae, recombinant, lyophilized - ECPY001
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. Carboxypeptidase Y has been obtained from yeast S. cerevisiae, has a broad substrate specificity and can therefore be used in sequence analysis of proteins. Carboxypeptidase Y has a temperature optimum in the 20 – 30 °C range and pH optimum between pH 6 and 7.C. rugosa Lipase 01, CRL 1 from Candida rugosa - ELCR01
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The Lipase 01 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Transglutaminase from guinea pig liver
CAS:Transglutaminase (2.3.2.13) is an enzyme that catalyzes formation of isopeptide bonds between the γ-carboxamide groups ( -(C=O)NH2 ) of glutamine side chains and amino groups. The donor of the amino group is usually (but not always) an ε-amino group ( -NH2 ) of lysine residue. The reaction also releases ammonia: Gln-(C=O)NH2 + NH2-Lys → Gln-(C=O)NH-Lys + NH3One unit of transglutaminase will catalyze the formation of 1.0 μmole transglutamination product per min at pH 6.0 and 37 °C.Purezza:Min. 95%Protein disulfide isomerase from bovine liver
CAS:An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteinsFormula:C7H5Cl2NO5SPurezza:Min. 95%Peso molecolare:286.09 g/molFormaldehyde Dehydrogenase
CAS:Formaldehyde dehydrogenase (EC 1.2.1.46) is an enzyme that catalyzes the following reaction: formaldehyde + NAD+ + H2O ⇌ formate + NADH + H+ One unit of formaldehyde dehydrogenase will convert 1.0 µmole of formaldehyde to formic acid per minute at pH 7.5 and 37°C in the presence of NAD+.NAD+ is available here.alpha Amylase enzyme
Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Human pancreatic Alpha Amylase is supplied as clear, colorless to light yellow liquid solution at ≥400U/mL, specific activity ≥100 U/mg protein.Store at 2-8 °C on arrival.Purezza:Min. 95%C. rugosa Lipase 03, CRL 3 from Candida rugosa - ELCR03
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The Lipase 03 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Glutathione Reductase, baker's yeast
CAS:Glutathione Reductase, baker's yeast, is an enzyme derived from the yeast species *Saccharomyces cerevisiae*. This enzyme is sourced from baker's yeast, providing a renewable and consistent product for various biochemical applications. Its mode of action involves catalyzing the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), using NADPH as an electron donor. This reaction is crucial for maintaining the intracellular redox balance by regenerating GSH, the primary cellular antioxidant.α-N-Acetylglucosaminidase
CAS:α-N-Acetylglucosaminidase (recombinant Human NAGLU Protein), degrades heparan sulfate by hydrolysis of terminal GlcNAc resides in N-acetyl-alpha-D-glucosaminides of heparan sulfate.Activity is measured by its ability to hydrolyse 4-Nitrophenyl 2-acetamido-2-deoxy-a-D-glucopyranoside EN03208 or EM31027. The specific activity is >900 pmol/min/μg, as measured under the decribed conditions.Purezza:(Sds-Page) Min. 95%Adenylate Kinase 1, human, recombinant
Adenylate kinase 1 (EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction: ATP + AMP ⇔ 2 ADP One unit of Adenylate kinase 1 will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at optimum conditions.Purezza:Min. 95%Ubiquitin thiolesterase UCHL1
CAS:Ubiquitin thiolesterase UCHL1 (Ubiquitin carboxy-terminal hydrolase L1; EC 3.1.2.15) is an enzyme that hydrolyses small C-terminal ubiquitin adducts to regenerate ubiquitin.Superoxide dismutase PEG
Superoxide dismutase coupled to polyethylene glycol. Superoxide dismutase (EC 1.15.1.1) is an enzyme that catalyzes the following reaction: 2 H+ + 2 O2− → O2 + H2O2 thus converting an extremely reactive and cytotoxic superoxide radical into oxygen and (significantly less reactive) hydrogen peroxide.
Mannitol dehydrogenase from leuconostoc mesenteroides
CAS:Mannitol dehydrogenase (MDH, mannitol 2-dehydrogenase, EC 1.1.1.67) is an enzyme that catalyzes the following reaction: D-mannitol + NAD+ ⇌ D-fructose + NADH + H+ One unit of mannitol dehydrogenase will generate 1.0 μmole of D-fructose per min in the presence of NAD+ at pH 8.6 and 40°C. NAD+ is available here and NADH is available here, depending on whether you require the reaction to proceed from left to right or from righ to left, respectively.
Purezza:Min. 95%Ref: 3D-JAA00165
5UPrezzo su richiesta10UPrezzo su richiesta25UPrezzo su richiesta50UPrezzo su richiestaEUCODIS® CalB01 IA, engineered variant of Candida antarctica Lipase B, immobilized by adsorption on hydrophobic carrier - ELCB01IA
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The CalB01 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.Lipoprotein lipase
CAS:Lipoprotein lipase is a critical enzyme used to modulate lipid processing, primarily sourced from mammalian tissues. It functions by hydrolyzing triglycerides present in circulating chylomicrons and very low-density lipoproteins. This enzymatic process liberates free fatty acids, which can subsequently be utilized as energy by peripheral tissues or stored in adipose tissue. Lipoprotein lipase is pivotal in lipid metabolism, participating in maintaining homeostasis of plasma lipid levels.Purezza:Min. 95%Chymase
CAS:Chymase (alternative names mast cell protease 1, mast cell serine proteinase, skeletal muscle protease, EC 3.4.21.39) is a serine protease, found in mast cells and basophil granulocytes.Purezza:Min. 95%Pyruvate kinase (from Rabbit muscle), ammonium sulfate suspension
CAS:Pyruvate kinase (from Rabbit muscle), ammonium sulfate suspension is an enzyme product, which is a purified protein extracted from the muscle tissue of rabbits. This enzyme plays a crucial role in glycolysis, specifically catalyzing the transphosphorylation of phosphoenolpyruvate (PEP) to pyruvate, generating ATP from ADP in the process. This step is a key regulatory point in the glycolytic pathway, which is essential for cellular energy production.
Purezza:Min. 95%Luciferase from Vibrio fischeri
CAS:Luciferase enzymes sourced from Vibrio fischeriColore e forma:PowderRibonuclease A
CAS:Ribonuclease A (RNase A) is widely used to break down RNA in DNA purification. RNase A catalyzes the endonucleolytic cleavage of phosphodiester bonds of RNA.
