Peroxidase, Maleimide Activated from horseradish

For direct conjugation to compounds containing free sulfhydryl groups for use as an enzyme-linked detection reagent.
Instructions for use included. In a study on horseradish peroxidase, the Maleimide compounds succinimidyl 4-maleimidobutyrate and succinimidyl 6-maleimidohexanoate have been shown to be the most effective in the conjugation of Fab′ to horseradish peroxidase. This enzyme has also been used in a study to investigate the effectiveness in staining a mitochondrial protein, lipoamide dehydrogenase.

To increase signal intensity of immunoconjugates, immunoglobulins were synthetically modified to contain multiple primary amines and covalently coupled to maleimide activated peroxidase. This can result in more efficient conjugation and signal amplification.

Peroxidase (POD) helps in the dehydrogenation of several organic compounds like phenols, aromatic amines, hydroquinones etc.

Peroxidase (POD) is an enzyme that includes a group of specific enzymes such as nicotinamide adenine dinucleotide (NAD) peroxidase, NADP peroxidase, fatty acid peroxidase and a group of non-specific enzymes from various sources. It is present in animals, higher plants and other organisms.

One unit will form 1.0 mg of purpurogallin from pyrogallol in 20 seconds at pH 6.0 at 20°C.

Type VI peroxidase activated with maleimidocaproic acid N-hydroxysuccinimide ester.

Lyophilized powder containing trehalose and sodium citrate