Non-toxic ready-to-use zinc-containing metallothionein-1. Cadmium ions, which are present due to the protein production in animals, were removed quantitatively and replaced by the natively occurring zinc ions (only traces of Cd, Cu remain). Suited for life science research including cell culture studies.
Product Details
| Alternative Name: | MT-1, MT-I, MT-1A, Zn7-MT-1 |
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| MW: | 6145 (without Zn); 6603 (incl. 7 Zn). |
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| Source: | Isolated from rabbit liver. |
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| UniProt ID: | P11957 (MT-1A) |
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| Concentration: | ~1000µg/ml |
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| Formulation: | Liquid. In 25mM TRIS/HCl, pH 8.0, containing 50mM NaCl. |
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| Purity: | ≥95% |
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| Quality Control: | SDS-PAGE, Cu/Cd/Zn-AAS, UV/VIS |
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| Shipping: | Blue Ice |
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| Short Term Storage: | +4°C |
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| Long Term Storage: | -20°C |
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| Handling: | For maximum product recovery after thawing, centrifuge the vial before opening the cap. Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C. |
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| Scientific Background: | MT-1 is an isoform of the ubiquitously occurring metalloproteins characterized by a high metal and cysteine sulphur content. It is composed of a single polypeptide chain of 61 amino acids, 20 of which are cysteine residues and none of which are aromatic amino acids or histidine. The MT-1 fraction contains additional MT isoforms, which differ only in amino acid residues other than Cys. They are similar in sequence and therefore also in charge. The 3D structure of the metal complex contains two separate domains, alpha and beta. The alpha-domain encloses four bivalent metal ions in the form of a Me4Cys11 cluster. The beta-domain contains an analogous Me3Cys9 cluster. Monovalent metal ions like Cu(I) can form a cluster as well, via thiolate bonds. Much of our understanding of the biological actions of MTs has arisen from the comparative analysis of the chemical and structural features. MT-1 is expressed in almost all tissues. It is a cytosolic protein, which is up-regulated in response to many factors, including metals, hormones, inflammation related stimuli (cytokines), and stressful reagents. It is suggested that it has multiple biological roles such as, regulatory role of Zn-metabolism (zinc-finger transcription factors), regulation of metal-exchange detoxification (marker for heavy metal intoxication), protection against reactive oxygen species (ROS), adaptation to stress, anti-apoptotic effects (activation of NF-κB/interaction with p50 subunit), and in protection against anticancer treatments. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Zinc supplementation can reduce accumulation of cadmium in aged metallothionein transgenic mice: K. Pabis, et al.; Chemosphere
211, 855 (2018),
Abstract;
Metallothionein, oxidative stress and trace metals in gills and liver of demersal and pelagic fish species from Kuwaits' marine area: M.U. Beg, et al.; Mar. Pollut. Bull.
100, 662 (2015),
Abstract;
Repeated exposure to Ochratoxin A generates a neuroinflammatory response, characterized by neurodegenerative M1 microglial phenotype: J.S. Tobel, et al.; Neurotoxicology
44, 61 (2014),
Abstract;
Scanning protein analysis of electrofocusing gels using X-ray fluorescence: S. Matsuyama, et al.; Metallomics
5, 492 (2013),
Abstract;
Spectrophotometric detection of labile zinc(II) released from metallothionein: a simple method to evaluate heavy metal toxicity: T. Asano, et al.; J. Biosci. Bioeng.
109, 638 (2010),
Abstract;
Large-scale preparation of metallothionein: biological sources: M. Vasak; Methods Enzymol.
205, 39 (1991),
Abstract;
Standard isolation procedure for metallothionein: M. Vasak; Meth. Enzymol.
205, 41 (1991),
Abstract;
General Literature References
Roles of the metallothionein family of proteins in the central nervous system: J. Hidalgo, et al.; Brain Res. Bull.
55, 133 (2001), (Review),
Abstract;
Nuclear localization of metallothionein during cell proliferation and differentiation: M.G. Cherian & M.D. Apostolova; Cell. Mol. Biol.
46, 347 (2000), (Review),
Abstract;
Primary structures of seven metallothioneins from rabbit tissue: P.E. Hunziker, et al.; Biochem. J.
306, 265 (1995),
Abstract;
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