9074-14-0

Basic information

• Product Name: RYNTR
• Synonyms: THIOREDOXIN: NADP+ OXIDOREDUCTASE;THIOREDOXIN REDUCTASE;THIOREDOXIN REDUCTASE RAT LIVER;THIOREDOXIN REDUCTASE, YEAST, RECOMBINANT;THIOREDOXIN REDUCTASE, YEAST, RECOMBINANT, E COLI;RYNTR;NADPH:OXIDISED THIOREDOXIN OXIDOREDUCTASE;NADPH: OXIDIZED THIOREDOXIN OXIDOREDUCTASE
• CAS NO: 9074-14-0
• Molecular Weight: 0
• Product Categories: enzyme
• Mol File: 9074-14-0.mol
• Article Data: 0

Chemical Properties

• Appearance: /buffered aqueous glycerol solution
• Storage Temp.: 2-8°C
• CAS DataBase Reference: RYNTR(CAS DataBase Reference)
• NIST Chemistry Reference: RYNTR(9074-14-0)
• EPA Substance Registry System: RYNTR(9074-14-0)

Safety Data

• Safety Statements: 23-24/25
• WGK Germany: 1
• Hazardous Substances Data: 9074-14-0(Hazardous Substances Data)

Usage

Description

RYNTR, also known as Thioredoxin Reductase from rat liver, is an enzyme that plays a crucial role in maintaining the redox balance within cells. It possesses reducing capacity and is involved in various cellular processes, making it a valuable tool for scientific research and potential therapeutic applications.

Uses

Used in Pharmaceutical Research:
RYNTR is used as a research tool for studying the uptake and reduction of a-lipoic acid by utilizing the reducing capacity of human erythrocytes. This helps in understanding the mechanisms of a-lipoic acid and its potential therapeutic applications.
Used in Biochemical Research:
RYNTR is used as a research tool for studying the activation mechanism of transglutaminase 2 (TG2) in the extracellular matrix by using Thioredoxin. This aids in understanding the role of TG2 in various biological processes and its potential as a therapeutic target.

Biochem/physiol Actions

Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxide.