GSTM3 Human
Glutathione S-Transferase MU 3 Human Recombinant
Cat. No.
BT7319
Source
E.coli.
Synonyms
Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione
S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.
S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
GSTM3 Recombinant produced in E. coli is a single polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 29.1kDa.
GSTM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GSTM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
GSTM3, a member of the glutathione s-transferase (GST) family, plays a crucial role in cellular detoxification. GSTs are categorized into eight families (alpha, kappa, mu, omega, pi, sigma, theta, and zeta), each with distinct functions. GSTM3, belonging to the mu family, specializes in detoxifying electrophilic compounds by conjugating them with glutathione. These compounds encompass various harmful substances, such as therapeutic drugs, carcinogens, environmental toxins, and oxidative stress products.
Description
Recombinant GSTM3, expressed in E. coli, is a single polypeptide chain with a molecular weight of 29.1 kDa. It consists of 249 amino acids, including a 24 amino acid His-tag at the N-terminus (amino acids 1-225). Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear and colorless solution, sterilized by filtration.
Formulation
The GSTM3 solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 100 mM NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 95% by SDS-PAGE analysis.
Synonyms
Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione
S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.
S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC
Product Science Overview
Structure and Function
GSTM3 is a cytosolic enzyme that is part of a larger family of GSTs, which are divided into several classes based on their biochemical, immunologic, and structural properties. The mu class, to which GSTM3 belongs, is involved in the detoxification of electrophilic compounds, including:
- Carcinogens
- Therapeutic drugs
- Environmental toxins
- Products of oxidative stress
These compounds are detoxified through conjugation with glutathione, a tripeptide that acts as an antioxidant .
Genetic Information
Recombinant Expression
Clinical Significance
Mutations in the GSTM3 gene have been linked to a slight increase in the risk of certain cancers, likely due to exposure to environmental toxins. Additionally, GSTM3 is associated with pathways involved in biotransformation and glutathione conjugation, which are critical for cellular defense mechanisms .
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