© 2008 Alexis Corporation
ALX-202-070 Revised 10-Jun-05
Metallothionein-1 (rabbit liver)
Add to Clipboard
SYNONYMS MT-1 (rabbit liver)
MT-I (rabbit liver)
MT-1A (rabbit liver)
Zn7-MT-1 (rabbit liver)
PRODUCT LINE Oxidative Stress
PRODUCT CATEGORY Antioxidants, Flavonoids & Free Radical Scavengers Other Products
Ordering Information
Product Numbers: Format: Size: Unit Price: Quantity: Add To Cart
ALX-202-070-C500   500 µg 195.00 USD Add To Cart
Product Specification
MW: 6145 (without Zn); 6603 (incl. 7 Zn).
SOURCE/HOST: Isolated from rabbit liver. Mixture of MT isoforms. Contains mainly MT-1a and MT-2e and a minor portion of MT-2d. [1]
CONCENTRATION: 590µg/ml
PURITY: ≥95%. ~7 Zn per molecule.
PURITY DETAIL: Essentially free of cadmium and copper (Cd in traces, <0.2 Cu/molecule).
FORMULATION: Liquid. In 25mM TRIS/HCl, pH 8.0, containing 50mM NaCl.
QUALITY CONTROL: SDS-PAGE, Cu/Cd/Zn-AAS, UV/VIS
SHIPPING: SHIPPED ON BLUE ICE
SHORT TERM STORAGE: +4°C
LONG TERM STORAGE: -20°C
HANDLING: Avoid freeze/thaw cycles. For maximum product recovery after thawing, centrifuge the vial before opening the cap. After opening, prepare aliquots and store at -20°C.
Product Description
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 Specific Literature References
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 Information
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. [2, 3]

General Literature References
[1] Primary structures of seven metallothioneins from rabbit tissue: P.E. Hunziker, et al.; Biochem. J. 306, 265 (1995) Abstract
[2] Nuclear localization of metallothionein during cell proliferation and differentiation: M.G. Cherian & M.D. Apostolova; Cell. Mol. Biol. 46, 347 (2000), (Review) Abstract
[3] Roles of the metallothionein family of proteins in the central nervous system: J. Hidalgo, et al.; Brain Res. Bull. 55, 133 (2001), (Review) Abstract
Further Categories Containing This Product:
Cell Death / Apoptosis / Autophagy Other ProductsNatural Proteins