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Key Documents

Altri documenti

GS39

Sigma-Aldrich

GST T2-2, Recombinant Rat

Sinonimo/i:

glutathione S-transferase, theta 2

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.26

Origine biologica

rat

Livello qualitativo

100

Ricombinante

expressed in E. coli

Saggio

>95% (SDS-PAGE)

Forma fisica

frozen liquid

Attività specifica

13.18 (using spectrophotometric determination of NADPH oxidation coupled to the glutathione peroxidase activity of GST T2-2 on cumene hydroperoxide (1.5 mM) in the presence of reduced glutathione (1 mM) in 100 mM NaPO4 (pH 7.0) at room temperature.)

PM

23 kDa

Concentrazione

2.44 mg/mL

Temperatura di conservazione

−70°C

Informazioni sul gene

rat ... Gstt2(29487)

Azioni biochim/fisiol

Glutathione S-transferase theta 2 (Gstt2) is an enzyme that in rats is encoded by the Gstt2 gene. Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTs are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.

Stoccaggio e stabilità

The enzyme should be used by the end-user customer within 1 year of receipt.

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

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P Jemth et al.
The Biochemical journal, 316 ( Pt 1), 131-136 (1996-05-15)
Rat glutathione transferase (GST) T2-2 of class Theta (rGST T2-2), previously known as GST 12-12 and GST Yrs-Yrs, has been heterologously expressed in Escherichia coli XLI-Blue. The corresponding cDNA was isolated from a rat hepatoma cDNA library, ligated into and
E M Van Lieshout et al.
Biochimica et biophysica acta, 1381(3), 305-311 (1998-09-05)
Nonsteroidal anti-inflammatory drugs (NSAIDs) have been claimed to reduce cancer rates in oesophagus, stomach and colon of humans and laboratory animals. Recently we showed that dietary administration of NSAIDs enhanced glutathione S-transferase (GST) class alpha, mu and pi levels in
Robert Fledrich et al.
Brain : a journal of neurology, 135(Pt 1), 72-87 (2011-12-23)
Charcot-Marie-Tooth disease is the most common inherited neuropathy and a duplication of the peripheral myelin protein 22 gene causes the most frequent subform Charcot-Marie-Tooth 1A. Patients develop a slowly progressive dysmyelinating and demyelinating peripheral neuropathy and distally pronounced muscle atrophy.
R C Strange et al.
Toxicology letters, 112-113, 357-363 (2000-03-18)
The glutathione S-transferases (GST) are a supergene family of dimeric, enzymes that catalyse the conjugation of glutathione (GSH) to a variety of electrophiles including arene oxides, unsaturated carbonyls, organic halides and other substrates. Their importance is suggested by the finding
Marjorie Coggan et al.
The Biochemical journal, 366(Pt 1), 323-332 (2002-06-01)
A novel Theta class glutathione transferase (GST) isoenzyme from mouse termed mGSTT3 has been identified by analysis of the expressed sequence tag database. The gene encoding mGSTT3 is clustered with the mGSTT1 and mGSTT2 genes on chromosome 10 and has

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