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Transthyretin is one of the three major thyroid hormone-binding proteins in plasma and/or cerebrospinal fluid of vertebrates. It exists mainly as a homotetrameric protein of approximately 55 kDa in plasma and, in sera and cerebrospinal fluid, is a carrier of the thyroid hormone thyroxine (T4) and retinol. While mostly known for being the transporter of thyroxine and retinol, when mutated, TTR is also well-described as the cause of familial amyloid polyneuropathy, a neurodegenerative lethal disorder characterized by systemic deposition of TTR amyloid fibrils, particularly in the peripheral nervous system. Recently, studies have shown that TTR has an important function development of peripheral and central nervous system physiology, namely by participating in behavior, in the maintenance of normal cognitive processes during ageing, amidated neuropeptide processing and nerve regeneration. Additionally, it has been proposed that TTR is neuroprotective in Alzheimer's disease, by preventing the formation of amyloid beta fibrils (Fleming C.E. et al. (2009) Prog Neurobiol., Epub ahead of print
References
Product Information
Format
Purified
Control
Human placenta lysate
Presentation
Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
This gene encodes transthyretin, one of the three prealbumins including alpha-1-antitrypsin, transthyretin and orosomucoid. Transthyretin is a carrier protein; it transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. The protein consists of a tetramer of identical subunits. More than 80 different mutations in this gene have been reported; most mutations are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart, and a small portion of the gene mutations is non-amyloidogenic. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, carpal tunnel syndrome, etc. [provided by RefSeq]
FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
SUBUNIT STRUCTURE: Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accomodate two ligand molecules. Interacts with RBP4.
SUBCELLULAR LOCATION: Secreted. Cytoplasm.
TISSUE SPECIFICITY: Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver.
DOMAIN: Each monomer has two 4-stranded beta sheets and the shape of a prolate ellipsoid. Antiparallel beta-sheet interactions link monomers into dimers. A short loop from each monomer forms the main dimer-dimer interaction. These two pairs of loops separate the opposed, convex beta-sheets of the dimers to form an internal channel.
INVOLVEMENT IN DISEASE: Defects in TTR are the cause of amyloidosis type 1 (AMYL1) [MIM:176300]. AMYL1 is a hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis.
Defects in TTR are the cause of amyloidosis type 7 (AMYL7) [MIM:105210]; also known as leptomeningeal amyloidosis or meningocerebrovascular amyloidosis. AMYL7 is a form of hereditary transthyretin amyloidosis characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. Mild systemic amyloidosis may occurr.
Defects in TTR are a cause of hyperthyroxinemia [MIM:176300].
MISCELLANEOUS: Tetramer dissociation and partial unfolding leads to the formation of aggregates and amyloid fibrils. Small molecules that occupy at least one of the thyroid hormone binding sites stabilize the tetramer, and thereby stabilize the native state and protect against misfolding and the formation of amyloid fibrils.
Two binding sites for thyroxine are located in the channel. Less than 1% of plasma prealbumin molecules are normally involved in thyroxine transport. L-thyroxine binds to the transthyretin by an order of magnitude stronger than does the triiodo-L-thyronine. Thyroxine-binding globulin is the major carrier protein for thyroid hormones in man.
About 40% of plasma transthyretin circulates in a tight protein-protein complex with the plasma retinol-binding protein (RBP). The formation of the complex with RBP stabilizes the binding of retinol to RBP and decreases the glomerular filtration and renal catabolism of the relatively small RBP molecule. There is evidence for 2 binding sites for RBP, one possibly being a region that includes Ile-104, located on the outer surface of the transthyretin molecule.
SEQUENCE SIMILARITIES: Belongs to the transthyretin family.
Molecular Weight
Transthyretin exists mainly as a homotetrameric protein of approximately 55 kDa in plasma. A single band of ~26 kDa was observed, which is an approximate size of a dimeric component that makes up the said homotetramer.
Physicochemical Information
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Materials Information
Toxicological Information
Safety Information according to GHS
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Product Usage Statements
Quality Assurance
Evaluated by Western Blot in human placenta lysate.
Western Blot Analysis: 2 µg/ml of this antibody detected Transthyretin in 10 µg of human placenta lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
