Enzima

Lipoxidase, from glycine max (soybean)

Oxalate Oxidase, freeze-dried, from Wheat is an enzyme preparation which is derived from wheat and functions through the oxidative degradation of oxalate. This enzyme catalyzes the conversion of oxalate into carbon dioxide and hydrogen peroxide, utilizing oxygen as a co-substrate in the process. The activity of Oxalate Oxidase is crucial in biological and biochemical applications where oxalate degradation is required.

Ubiquitin Conjugating enzyme E2C (other names UBE2C, UBCH10, dJ447F3.2, ubiquitin conjugating enzyme E2 C; EC 2.3.2.24) is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UBE2C bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UBE2C is useful for in vitro ubiquitinylation reactions.

Protein phosphatase 2C is a key enzyme, which is a serine/threonine-specific phosphatase, derived from various organisms including humans, plants, and bacteria. This enzyme plays a pivotal role in cellular signaling by removing phosphate groups from serine and threonine residues on target proteins, a process known as dephosphorylation. This action is crucial for the regulation of diverse cellular functions, including stress responses, cell division, and apoptosis.

<p>Nitrilase (nitrile aminohydrolase; EC 3.5.5.1) in an enzyme that catalyzes hydrolysis of nitriles to carboxilic acids and ammonia:  R-CN + 2 H2O → R-COO- + NH4+  One unit of nitrilase will yield 1.0 μmol of ammonia per minute under optimal reaction conditions using acrylonitrile as a substrate.</p>

Butyrylcholinesterase (BCHE, BuChE, PCHE, pseudocholinesterase, plasma cholinesterase, Acylcholine acyl-hydrolase, Choline esterase; EC 3.1.1.8, CAS No [9001-08-5]) is an enzyme that made in the liver and found mainly in blood plasma. It catalyzes the following reaction: Acylcholine + H2O → choline + carboxylic acidOne unit of Butyrylcholinesterase will change absorbance by 0.2 milliunits (mA) per minute at optimal buffer conditions and 37 ̊C. Equine serum butyrylcholinesterase is supplied as white to pale grey-green powder with activity of ≥50U/mg and specific activity of ≥300U/mg protein. It can be dissolved at 5 mg/mL concentration in 50 mM Tris-HCl pH 7.3 - 7.5, giving colorless to slightly green solution. Equine serum butyrylcholinesterase is activated by Ca2+, optimum pH 7-8, KM=18 µM (butyrylthiocholine at 25°C). Store at -20°C on arrival.

Hyaluronidase is an enzymes that catalyses the degradation of hyaluronic acid.

Alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the following chemical reaction: a primary alcohol + O2 + H2O ⇌ an aldehyde + H2O2   One unit of alcohol oxidase will oxidize 1.0 µmole of methanol to formaldehyde per min at pH 7.5 and 25 °C.

<p>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 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>

<p>Citrate synthase (E.C. 2.3.3.1) is an enzyme that catalyzes the following reaction: acetyl-CoA + oxaloacetate + H2O → citrate + CoA-SHOne unit of citrate synthase will form 1.0 μmole of citrate from acetyl-CoA and oxalacetate per min at pH 8.0 and 37 °C.Origin is porcine heart.Molecular weight ~ 49kDa (monomer) and  ~ 98kDa (dimer)</p>

<p>Plasmin, human is a serin protease which present in the blood and is involved in the cleavage of cross-linked fibrin, a process known as fibrinolysis.One unit will produce one micromole of P-Nitroanilide from D-Val-Leu-Lys-P-Nitroanilide per minute at pH 7.5 at 37°C</p>

<p>Recombinant Isocitrate Dehydrogenase is a bioengineered enzyme, which is derived from microbial or eukaryotic expression systems designed to mirror its naturally occurring form. This enzyme catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate, utilizing NADP+ as a cofactor in the process. Its mode of action involves the conversion of isocitrate to alpha-ketoglutarate with the concomitant reduction of NADP+ to NADPH.</p>

<p>Aconitase catalyzes isomerization of citrate to isocitrate via cis-aconitate. Systemic enzyme name is aconitate hydratase; EC 4.2.1.3.</p>

<p>Creatinase (EC 3.5.3.3) is an enzyme that catalyzes the fellowing reaction: creatine + H2O ⇌ sarcosine + ureaOne unit of creatinase will hydrolyze 1.0 µmole of creatine into sarcosine and urea per min at pH 7.5 and 37 °C.</p>

<p>L-Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: L-Asparagine + H2O → L-Aspartate + NH4+   One unit will yield 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 and 37 °C.</p>

<p>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.</p>

Casein kinase 2 (CK2, CSNK2; EC 2.7.11.1) is a constitutively active serine and threonine protein kinase. It plays a role in a range of cellular processes, including DNA repair, cell cycle control, metabolic regulation, circadian rhythms and more. Its known substrates include hundreds of proteins. One unit of CK2 will phosphorylate of 1 pmol of of peptide substrate in 1 minute at 30°C and presence of ATP.

<p>Thermostable β-Glucanase 2 is an enzyme that hydrolases β-Glucans into glucose. One unit of β-Glucanase 2 will produce 1.0 μmole of glucose from β-glucan per minute at pH 5.8 and 70 °C.</p>

<p>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 CalB02 ICE lipase has been immobilized on a hydrophobic carrier by a covalent linkage. The immobilized CalB02 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>

<p>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 ICE lipase has been immobilized on a hydrophobic carrier by a covalent linkage. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>