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Human Polyclonal TTR Primary Antibody for IF (p), IHC (p) - ABIN725540
Liu, Zhao, Lu, Fan, Wang: Proteomic study on usnic-acid-induced hepatotoxicity in rats. in Journal of agricultural and food chemistry 2012
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Human Polyclonal TTR Primary Antibody for IHC, IHC (p) - ABIN4362157
Noborn, OCallaghan, Hermansson, Zhang, Ancsin, Damas, Dacklin, Presto, Johansson, Saraiva, Lundgren, Kisilevsky, Westermark, Li: Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein. in Proceedings of the National Academy of Sciences of the United States of America 2011
Show all 3 Pubmed References
Human Polyclonal TTR Primary Antibody for IHC, ELISA - ABIN1585446
Sourisseau, Goldman, He, Gori, Kiem, Gouon-Evans, Evans: Hepatic cells derived from induced pluripotent stem cells of pigtail macaques support hepatitis C virus infection. in Gastroenterology 2013
Show all 2 Pubmed References
Human Polyclonal TTR Primary Antibody for ELISA - ABIN2481284
Beetham, Dawnay, Ghany, Dubrey, Miles: A radioimmunoassay for human urinary prealbumin. in Annals of clinical biochemistry 1993
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Mouse (Murine) Polyclonal TTR Primary Antibody for ICC, IHC - ABIN1078614
Murakami, Sango, Watabe, Niimi, Takaku, Li, Yamamura, Sunada: Schwann cells contribute to neurodegeneration in transthyretin amyloidosis. in Journal of neurochemistry 2015
Human Polyclonal TTR Primary Antibody for ELISA, EIA - ABIN251465
Sekijima, Wiseman, Matteson, Hammarström, Miller, Sawkar, Balch, Kelly: The biological and chemical basis for tissue-selective amyloid disease. in Cell 2005
The results suggest an association between presumed nonamyloidogenic mutations in the TTR gene and the development of autonomic and small fiber neuropathy.
Clinical, electrophysiological, histopathological, and genetic characteristics of 17 patients from Turkey (5 female, 13 male) from nine families with polyneuropathy and mutations in TTR were evaluated. Sequence analysis of the TTR gene revealed five mutations (Val30Met, Glu89Gln, Gly53Glu, Glu54Gly and Gly47Glu). Study suggests that a cohort of patients from Turkey with TTR-FAP exhibits clinical and genetic heterogeneity.
It is one of the major Abeta (show APP Antibodies)-binding proteins acting as a neuroprotector in AD. In addition, TTR cleaves Abeta (show APP Antibodies) peptide in vitro.
Stroke patients with lower transthyretin levels had poorer Functional Independence Measure outcomes and tended not to be discharged to their own homes.
TTR expression varied across human populations
Cell-based experiments showed that overexpression of TTR could improve HK-2 cell viability and inhibit apoptosis.
These results clarify a negligible degree of unfolding of beta-strand C in the formation of the amyloidogenic state and establish the concept that TTR is a highly plastic protein able to populate at least three distinct conformational states.
A strong phenotypic heterogeneity was demonstrated across coding mutations causing TTR amyloidosis. Non-coding variants affect TTR expression and, consequently, phenotypic presentation in carriers of amyloidogenic mutations.
Serum prealbumin was significantly lower in patients with versus those without post-stroke depression, and was a significant predictor of post-stroke depression after adjusting for confounding risk factors.
TTR induced apoptosis of retinal microvascular endothelial cells in an environment that simulated hypoxia.
This study reports a possible mechanism for Rhabdomyolysis-Induced Acute Kidney Injury and suggests that reductions in TTR could increase the generation of Reactive Oxygen Species and induce apoptosis.
TTR neuritogenic activity is mediated by the megalin (show LRP2 Antibodies) receptor and is lost in megalin (show LRP2 Antibodies)-deficient neurons.
New insights into ghrelin (show GHRL Antibodies) cell physiology, and given the known functions of RBP4 (show RBP4 Antibodies) and TTR, support an emerging role for the ghrelin (show GHRL Antibodies) cell in blood glucose handling and metabolism.
Transthyretin (TTR) deposition in the peripheral nervous system is the hallmark of familial amyloidotic polyneuropathy (FAP (show FAP Antibodies)).
TTR mediated transport of thyroxine represents a survival mechanism necessary for the myogenic program.
provide evidence of a new role of Transthyretin as a transcription inducer of insulin (show INS Antibodies)-like growth factor receptor (show RYK Antibodies) I in central nervous system, unveiling a new role in neuroprotection
data also indicate that it is unlikely that the behaviors seen in Ttr(-/-) mice are related to its function
Native transthyretin inhibits all preeclampsia-like features in the humanized mouse model.
Transthyretin silencing (TTRkd) significantly reduced myogenin (show MYOG Antibodies) expression.
Amyloid fibrils formed by a mutant form of TTR, A25T, activate microglia, leading to the secretion of tumor necrosis factor-alpha (TNF-alpha (show TNF Antibodies)), interleukin-6 (IL-6 (show IL6 Antibodies)) and nitric oxide.
The rank order potency of the chemicals tested for the displacement of [125I]TIP from TTR was TIP > ioxynil > pentachlorophenol, T4, and retinoic acid > tetrabromobisphenol A, diethylstilbestrol, and T3.
This study suggested closer links between the release of haptoglobin (show HP Antibodies), Pig-MAP and monocytes compared to the release of AGP, SAA (show SAA1 Antibodies) and transthyretin.
Study determined the genomic structure of the Xenopus laevis TTR gene including 5'-flanking regions, and examined TTR expression patterns in several tissues; coding regions of xTTR gene was separated into 4 exons by 3 introns and these numbers were in agreement with those determined for the human, mouse, and rat genes
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.
, transthyretin (prealbumin, amyloidosis type I)
, transthyretin (prealbumin, amyloidosis type 1)
, carpal tunnel syndrome 1
, prealbumin, amyloidosis type I
, thyroxine-binding prealbumin