chemical-categories

Cholesterol Oxidase, PEG Modified LAB GRADE 1

PEG (Polyethylene glycol) modified cholesterol oxidase (Cholesterol oxidase PEG) is one of our premier cholesterol oxidase conjugates. Cholesterol oxidase is an enzyme that catalyzes the oxidation of cholesterol by oxygen into cholest-4-en-3-one and H2O2. This enzyme belongs to the family of oxidoreductases. Cholesterol oxidase has been used widely in the determination of serum cholesterol combined with other enzymes. PEG modified cholesterol oxidase provides better stability of this enzyme without major compromising its bioactivity. All our labeled cholesterol oxidase products were performed under mild reaction conditions to retain their maximum bioactivity. These conjugates were further purified by chromatography to ensure adequate applications both in-vitro and in-vivo.

PEG (Polyethylene glycol) modified cholesterol oxidase (Cholesterol oxidase PEG) is one of our premier cholesterol oxidase conjugates. Cholesterol oxidase is an enzyme that catalyzes the oxidation of cholesterol by oxygen into cholest-4-en-3-one and H2O2. This enzyme belongs to the family of oxidoreductases. Cholesterol oxidase has been used widely in the determination of serum cholesterol combined with other enzymes. PEG modified cholesterol oxidase provides better stability of this enzyme without major compromising its bioactivity. All our labeled cholesterol oxidase products were performed under mild reaction conditions to retain their maximum bioactivity. These conjugates were further purified by chromatography to ensure adequate applications both in-vitro and in-vivo.

Native Aspergillus niger Catalase LAB GRADE 1

Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis.

UDP-acetylglucosamine deacetylase LAB GRADE 1

UDP-acetylglucosamine deacetylase is a metal-dependent deacetylase from Escherichia coli that removes the acetyl group from the 2-amino group of UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine (myr-UDP-GlcNAc)3.

UDP-acetylglucosamine deacetylase is a metal-dependent deacetylase from Escherichia coli that removes the acetyl group from the 2-amino group of UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine (myr-UDP-GlcNAc)3.

Lytic polysaccharide monooxygenase LAB GRADE 1

Lytic chitin monooxygenase is a copper-dependent lytic polysaccharide monooxygenase (LPMO). Copper-dependent lytic polysaccharide monooxygenases (LPMOs) are key players in the enzymatic conversion of biomass. LPMOs catalyze oxidative cleavage of glycosidic bonds in a process involving molecular oxygen and an electron donor, such as cellobiose dehydrogenase (CDH).

Adenosine 5'-triphosphate (sodium salt) LAB GRADE 95

Peptidoglycan N-acetylglucosamine deacetylase LAB GRADE 1

Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase) is an enzyme with systematic name peptidoglycan-N-acetylglucosamine amidohydrolase. This enzyme catalyses the following chemical reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O → peptidoglycan-D-glucosamine + acetate. This enzyme contributes to virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.

Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase) is an enzyme with systematic name peptidoglycan-N-acetylglucosamine amidohydrolase. This enzyme catalyses the following chemical reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O → peptidoglycan-D-glucosamine + acetate. This enzyme contributes to virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.

3-galactosyl-N-acetylglucosaminide 4-L-fucosyltransferase LAB GRADE 1

This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-α-fucosylation of the GlcNAc in β-D-Gal-(1→3)-β-GlcNAc sequences (with some activity also as 3-α-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-α- and 4-α-fucosyltransferase activities.

This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-α-fucosylation of the GlcNAc in β-D-Gal-(1→3)-β-GlcNAc sequences (with some activity also as 3-α-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-α- and 4-α-fucosyltransferase activities.

Heparosan synthase from Pasteurella multocida, Recombinant LAB GRADE 1

Heparosan synthase [pmHS enzyme] catalyzes transfer of GlcUA and GlcNAc to heparosan chain.

Porphyranase 16A from Zobellia galactanivorans, Recombinant LAB GRADE 1

Beta-porphyranase (EC 3.2.1.178, porphyranase, PorA, PorB, endo-beta-porphyranase) is an enzyme with systematic name porphyran beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate 4-glycanohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran. The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate.

Beta-porphyranase (EC 3.2.1.178, porphyranase, PorA, PorB, endo-beta-porphyranase) is an enzyme with systematic name porphyran beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate 4-glycanohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran. The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate.

Rhamnogalacturonan Lyase from Cellvibrio japonicus, Recombinant LAB GRADE 1

Rhamnogalacturonan Lyase is an endo-1,4-α-rhamnogalacturonan lyase. This enzyme catalyses the following chemical reaction: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.

Rhamnogalacturonan Lyase is an endo-1,4-α-rhamnogalacturonan lyase. This enzyme catalyses the following chemical reaction: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.