Succinate Dehydrogenase (SDH) (EC 1.3.5.1) or succinate-coenzyme Q reductase (SQR) or respiratory complex II is an enzyme complex, which is bound to the inner mitochondrial membrane. SDH participates in both the citric acid cycle and electron transport chain. In mammals and many bacteria, SDH consists of 2 hydrophilic subunits, SDHA (flavoprotein) and SDHB (iron-sulfur protein) and 2 hydrophobic membrane anchor subunits: SDHC and SDHD. SDH oxidizes succinate to fumarate and transfers the electrons to ubiquinone. SDH deficiency in humans leads to a variety of phenotypes including Leigh syndrome, a neurometabolic disorder, tumor formation, and myopathy. Recent studies show that SDH can prevent the generation of ROS (reactive oxygen species); therefore, measurement of succinate dehydrogenase activity has wide applications. The assay is initiated with the enzymatic hydrolysis of Succinic acid by SDH. The enzyme catalysed reaction products can be measured at a colorimetric readout at 600 nm.

Functional Assay

Succinate Dehydrogenase

100 Assays

1575.00

Pyruvate dehydrogenase (PDH) is a mitochondrial enzyme that catalyzes the conversion of pyruvate to acetyl-CoA and CO2, and also links the tricarboxylic acid (TCA) and glycolysis pathways. The enzyme is inhibited by phosphorylation and activated by dephosphorylation. Mutations in PDH have been linked to pyruvate dehydrogenase deficiency (causing lactic acidosis and neurologic dysfunctions) and Leigh syndrome. PDH has also been implicated in oncogeneinduced senescence. PDH measurements can provide insights into metabolic functions and oncogenesis. The assay is initiated with the enzymatic hydrolysis of Pyruvic acid by PDH. The enzyme catalysed reaction products can be measured at a colorimetric readout at 600 nm.

Functional Assay

Pyruvate Dehydrogenase

100 Assays

2756.25

Chymotrypsin is a digestive enzyme belonging to a super family of enzymes called serine proteases. It uses an active serine residue to perform hydrolysis on the C-terminus of the aromatic amino acids of other proteins. Chymotrypsin is a protease enzyme that cleaves on the C-terminal phenylalanine (F), tryptophan (W), and tyrosine (Y) on peptide chains. It shows specificity for aromatic amino acids because of its hydrophobic pocket. The assay is initiated with the enzymatic catalysis of ATEE by Chymotrypsin. The enzyme catalysed reaction products can be measured at a colorimetric readout at 237 nm.

Functional Assay

Chymotrypsin

100 Assays

2283.75

Chitinases (EC 3.2.1.14) are hydrolytic enzymes that break down glycosidic bonds in chitin. Chitinase catalyzes the hydrolytic cleavage of the beta-1→4-glycoside bond present in biopolymers of N-acetylglucosamine, primarily in chitin. Chitinases are widely distributed in living organisms and are found in fungi, bacteria, parasites, plants, and animals. They are classified in families based on amino acid sequence similarities. As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are generally found in organisms that either need to reshape their own chitin or dissolve and digest the chitin of fungi or animals. Chitinases perform different functions in different organisms. In bacteria, they are mainly involved in nutritional processes. In yeast and various fungi, these enzymes participate in morphogenesis. In animals and plants, chitinases primarily play a role in the defense of the organism against pathogen attack. The assay is initiated with the enzymatic hydrolysis of the chitin by chitinases. The enzyme catalysed reaction products N-acetylglucosamine react with PDAB, and can be measured at a colorimetric readout at 585 nm.

Functional Assay

Chitinase

100 Assays

2362.50

Beta-xylosidase (EC 3.2.1.37) is an enzyme with system name 4-beta-D-xylan xylohydrolase. This enzyme catalyses the following chemical reaction Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. This enzyme also hydrolyses xylobiose. The enzyme catalysed reaction products p-nitrophenol can be measured at a colorimetric readout at 405 nm.

Functional Assay

Beta-xylosidase

100 Assays

3071.25

Glucose (C6H12O6) is a key diagnostic parameter for many metabolic disorders. Increased glucose levels have been associated with diabetes mellitus, hyperactivity of thyroid, pituitary and adrenal glands. Decreased levels are found in insulin secreting tumors, myxedema, hypopituitarism and hypoadrenalism. The assay is initiated with the enzymatic catalysis of glucose by glucose oxidase. The enzyme catalysed reaction products H2O2 react with the substrate, and can be measured at a colorimetric readout at 505 nm.

Functional Assay

Glucose (Serum)

100 Assays

2362.50

Cellulases are a family of enzymes that include ß-Glucosidases, endoglucanases, and exoglucanases. These enzymes cleave the ß-1,4-D-glycosidic bonds that link the glucose units comprising cellulose. In addition to being produced by plants, cellulase activity is found in many fungi and bacteria, including some plant pathogens. Most animal cells are not known to produce cellulase; cellulolytic activity is often carried out in animals by symbionts. However, recent evidence does suggest cellulase production in some animals, such as insects and arthopods. The study of cellulase activity has many applications in plant molecular biology, agriculture, and manufacturing. Cellulase is also becoming important in the development of alternative fuel sources, as glucose obtained from cellulose hydrolysis is easily fermented into ethanol. The enzyme catalysed reaction products can be measured at a colorimetric readout at 540 nm.

Functional Assay

Cellulase

100 Assays

2450.00

Sorbitol dehydrogenase (SDH), found in organisms from bacteria to humans, converts sorbitol, the sugar alcohol form of glucose, to fructose, and the zinc-dependent reaction uses NAD+ as a cofactor. Organs abundant in SDH activity include the liver, kidney, lens and seminal vesicle. SDH and aldose reductase (AR) form the polyol pathway that interconverts glucose and fructose. Since SDH activity promotes the formation of NADH, the redox change induced by elevated SDH may have a pathogenic role in certain disease state, making SDH a potential therapeutic target. In addition, SDH has a close evolutionary relationship with alcohol dehydrogenase (ADH). The assay is initiated with the enzymatic hydrolysis of the sorbitol by sorbitol dehydrogenase. The enzyme catalysed reaction products NADH, can be measured at a colorimetric readout at 340 nm.

Functional Assay

Sorbitol Dehydrogenase

100 Assays

2450.00