|Application ||WB, IHC|
|Calculated MW||15887 Da|
|Other Names||Transthyretin, ATTR, Prealbumin, TBPA, TTR, PALB|
|Target/Specificity||A synthetic peptide corresponding to residues on the C-terminus of human Prealbumin was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Prealbumin Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.|
|Cellular Location||Secreted. Cytoplasm.|
|Tissue Location||Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver|
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Transthyretin (prealbumin/TTR) is a hormone-binding protein that participates in the plasma transport of both thyroxine and retinol (vitamin A). Transthyretin concentrations are disproportionately high in human ventricular CSF. It is reported to be either selectively transported across or synthesized within the blood-CSF barrier (3). Over 80 different disease-causing mutations in transthyretin have been reported. The vast majority is inherited in an autosomal dominant manner and is related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. A small portion of transthyretin mutations are apparently non-amyloidogenic (4). The human amyloid disorders, familial amyloid polyneuropathy, familial amyloid cardiomyopathy and senile systemic amyloidosis, are caused by insoluble transthyretin fibrils (2). Transthyretin has a structural complementarity to double-helical DNA, where the proposed binding site is composed of two symmetry-related beta-sheets containing a pair of helically disposed arms (1).
1. Blake CC, et al. Nature. 268(5616):115-20, 1977
2. Klabunde T, et al. Nat Struct Biol. 7(4):312-21, 2000
3. Herbert J, et al. Neurology 36(7):900-11, 1986
4. Saraiva MJ Hum Mutat. 17(6):493-503, 2001
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