Enzima

<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 lipase from the yeast Y. lipolytica has a temperature optimum in the 30 - 40 °C range and pH optimum between pH 7 and 8.</p>

<p>Endopeptidase, liquid, food grade, broad spectrum is an enzymatic product used in the food industry. It is derived from microbial sources, specifically engineered strains capable of producing high yields of proteolytic enzymes. This endopeptidase functions by hydrolyzing peptide bonds within proteins, targeting internal sites to break down long protein chains into smaller peptides and amino acids.</p>

<p>Endopeptidase, liquid, food grade is an enzymatic product that functions as a crucial component in the hydrolysis of protein substrates. This enzyme is typically derived from microbial sources, such as bacteria or fungi, and is cultivated under controlled fermentation processes to ensure high purity and activity levels. The primary mode of action of endopeptidases involves the cleavage of peptide bonds within protein molecules, effectively breaking down long protein chains into smaller peptides and amino acids.</p>

<p>beta lactamase I activity - min. 600.0 IU/mg</p>

<p>VIM-15 (β-Lactamase) is an enzyme product, specifically a metallo-beta-lactamase, which is sourced from certain resistant bacterial strains. This enzyme functions by hydrolyzing the beta-lactam ring of antibiotics, rendering them ineffective. The primary mode of action involves the coordination of zinc ions at its active site, enabling the breakdown of a broad spectrum of beta-lactam antibiotics including penicillins, cephalosporins, and carbapenems. This enzymatic activity significantly contributes to antibiotic resistance, posing a challenge in the treatment of bacterial infections. Its prevalence is noted in healthcare settings, where multidrug-resistant organisms are a concern. VIM-15 is of particular interest in clinical microbiology research and antimicrobial resistance studies, where understanding its structure and function can aid in the development of new inhibitors, potentially restoring the efficacy of beta-lactam antibiotics against resistant strains. Its characterization and study are critical for developing strategies to combat antibiotic-resistant infections effectively.</p>

Lipase 38 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at >50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 38 was shown to hydrolyze p-Nitrophenyl esters of acetate (27 % activity compared to butyrate), butyrate (100 %), octanoate (9 %) and caprate (5 %).

<p>LacBuster®-L is a novel liquid and ready-to-use sterile beta-lactamase formulation with a broad substrate range against beta-lactam antibiotics including carbapenems, cephalosporins up to 5th generation and penicillins. LacBuster®-L is especially well suited for the direct innoculation method and membrane filtration tests according to US Pharmacopeia (USP &lt;71&gt;) and European Pharmacopeia (EP &lt;2.6.1&gt;). 1 Piece contains 10 vials.</p>

<p>Catalyst for signal development in immunoassays</p>

<p>Alpha-L-iduronidase is a glycoside hydrolase enzyme that cleaves the non-reducing, terminal alpha-L-iduronic acid residues from polysaccharides and oligosaccharides. Alpha-L-iduronidase is involved in the lysosomal degradation of glycosaminoglycans and its deficiency leads to the accumulation of dermatan sulphate and heparan sulphate in tissues, a condition known as mucopolysaccharidosis I (MPS I). Alpha-L-iduronidase activity can be detected and quantified in an assay using a fluorogenic substrate 4MU-alpha-L-idopyranosiduronic acid. Alpha-L-iduronidase is also used in a 2-step assay for Hunter syndrome (MPS II) testing in combination with 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate.<br>This enzyme is supplied as a 2 mg/mL aqueous solution in 25 mM sodium acetate, 150 mM NaCl, 50% glycerol, pH 5.0 from a bacterial source, recombinantly expressed in Escherichia coli (see application notes for more details). Alpha-L-iduronidase is also available as lyophilisate (FA181881)</p>

<p>(R)-Mandelonitrile lyase (systematic name mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming), other names are D-oxynitrilase, D-alpha-hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, mandelonitrile benzaldehyde-lyase, ydroxynitrile lyase; EC 4.1.2.10) is the enzyme that catalyzes the following reaction:mandelonitrile ⇌ hydrogen cyanide + benzaldehydeOne unit of (R)-mandelonitrile lyase will convert 1.0 μmol of mandelonitrile per minute under optimal conditions.</p>

<p>PAIRED PRODUCTS AVAILABLE:</p>

<p>Lipase 04 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 60-70°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 04 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (68 %), laurate (2 %), palmitate (2 %), stearate (2 %), arachidate (2 %) and behenate (2 %).</p>

Lipase CR 03 is an industrial-grade enzyme product that is derived from microbial sources, specifically engineered for robust and efficient catalytic activity. The enzyme is extracted utilizing advanced fermentation techniques that capitalize on the prolific nature of specific strains known for lipase production. Its mode of action involves the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. This catalytic process is critical in various biochemical pathways and industrial reactions.

Lipase immo Kit 01 is an advanced biochemical tool designed for the immobilization of lipase, an enzyme commonly sourced from microorganisms. This innovative kit utilizes a sophisticated immobilization matrix to enhance enzyme stability and reusability. By binding the enzyme to a solid support, the kit facilitates repeated and continuous use in various reactions without significant loss of activity.

<p>Test sample of Cymit Quimica's Phospholipase D 040 Halal and Kosher Food grade bulk enzyme (EPLD840.6). With one of the most competitive activity rates on the global market and manufactured in Europe, this enzyme is perfect for use in food, diagnostic, therapeutic and nutraceutical industries worldwide.  Phospholipase D is an enzyme that is expressed in almost all types of organisms and whose activity can be harnessed to synthesize critical raw materials, for example phosphatidylserine. Phosphatidylserine has shown itself to be an important functional ingredient in reducing cognitive dysfunction and dementia in the field of nutraceuticals. As a Halal and Kosher food grade enzyme, Cymit Quimica's Phospholipase D is an excellent candidate for a diverse variety of food industry applications. Furthermore our enzyme can be used in diagnostic assays, creating first-class drug delivery systems and APIs. Product is a lyopholised solid</p>

PLA2G10 Protein, Rat, Recombinant (His & Myc) is expressed in E.

Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.

E3 ubiquitin ligase.

STK11 Protein, Human, Recombinant (His & SUMO) is expressed in E.

Cell wall formation.

GBA2 Protein, Rat, Recombinant (His) is expressed in E.

Catalyzes the phosphorylation of dihydroxyacetone.

SIRT6 Protein, Human, Recombinant (GST) is expressed in E.

UGT89C1 Protein, Arabidopsis thaliana, Recombinant (Yeast, His) is expressed in yeast with N-10xHis tag.

TIPARP Protein, Human, Recombinant (His) is expressed in Baculovirus.

Essential enzyme in the ergosterol biosynthetic pathway.

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Key enzyme for ketone body catabolism.

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the

Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp)

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A).

Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate.

Involved in the O-glucosylation of monolignols (alcohol monomers of lignin).

Zinc metalloproteinase aureolysin Protein, S.

Has pectate lyase activity.

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-

May have lyase activity.

Kallikrein 14 Protein, Mouse, Recombinant (His) is expressed in E. coli.

PDE9A Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

Catalyzes the deamidation of nicotinamide, an early step in the NAD(+) salvage pathway.

EIF3F Protein, Human, Recombinant (His) is expressed in E.

Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during

Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues,

PKM2 Protein, Rat, Recombinant (E.

Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential

Removes the formyl group from the N-terminal Met of newly synthesized proteins.

Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.

Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.

Catalyzes the hydrolysis of levan with endo-type specificity.

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan

DDX3X Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag.

HSPA5 Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 72.5 kDa and the accession number is P20029.

Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA.

Functions as glutathione transferase.

PRKN Protein, Rat, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag.

NOX4 Protein, Human, Recombinant (Cell-Free, His) is expressed in E.

SLFN12 Protein, Human, Recombinant (His) is expressed in in vitro E. coli expression system.

MMP-13 Protein, Human, Recombinant (His & SUMO) is expressed in E.

SVMP Protein, Bothrops atrox, Recombinant (His & Myc) is expressed in E.

NME4 Protein, Human, Recombinant (GST) is expressed in E.

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A).

GALNS Protein, Human, Recombinant (GST) is expressed in E.

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (

Diarrheal toxin that hydrolyzes gelatin, azocoll, actin, tropomyosin, and fibrinogen.

Putative phospholipase.

PIP4K2B Protein, Human, Recombinant (His) is expressed in E.

Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens.

PGK1 Protein, Cricetulus griseus, Recombinant (His) is expressed in Yeast.

Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline.

May be involved in tissue injury and remodeling.

Removes the N-terminal methionine from nascent proteins.

Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function.