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Human Polyclonal TTR Primary Antibody für 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 für 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
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Human Polyclonal TTR Primary Antibody für 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
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Human Polyclonal TTR Primary Antibody für ELISA - ABIN2481284
Beetham, Dawnay, Ghany, Dubrey, Miles: A radioimmunoassay for human urinary prealbumin. in Annals of clinical biochemistry 1993
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Human Polyclonal TTR Primary Antibody für ELISA, EIA - ABIN251465
Sekijima, Wiseman, Matteson, Hammarström, Miller, Sawkar, Balch, Kelly: The biological and chemical basis for tissue-selective amyloid disease. in Cell 2005
Mouse (Murine) Polyclonal TTR Primary Antibody für ICC, IHC - ABIN1078614
Murakami, Sango, Watabe, Niimi, Takaku, Li, Yamamura, Sunada: Schwann cells contribute to neurodegeneration in transthyretin amyloidosis. in Journal of neurochemistry 2015
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.
Data suggest that transthyretin exhibits site-specific solvation of the indole ring of tryptophans W41 and W79; these studies involved incorporation of tryptophan labeled with fluorine at 5 or 6 positions (5-fluorotryptophan/5FW or 6-fluorotryptophan/6FW) into recombinant TTR; replacement of fluorine at 5-position of a tryptophan with one at adjacent 6-position emphasizes delicate balance of stability in TTR tetramer.
This study shows that highly destabilized, aggregation-prone TTR variants are secreted as both native tetramers and non-native conformations that accumulate as high-molecular-weight oligomers.
The role of transthyretin in normal pregnancy is reviewed.
the role of H88 and the hydrogen bond network in the stability of TTR
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 (zeige LRP2 Antikörper) receptor and is lost in megalin (zeige LRP2 Antikörper)-deficient neurons.
New insights into ghrelin (zeige GHRL Antikörper) cell physiology, and given the known functions of RBP4 (zeige RBP4 Antikörper) and TTR, support an emerging role for the ghrelin (zeige GHRL Antikörper) cell in blood glucose handling and metabolism.
Transthyretin (TTR) deposition in the peripheral nervous system is the hallmark of familial amyloidotic polyneuropathy (FAP (zeige FAP Antikörper)).
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 (zeige INS Antikörper)-like growth factor receptor (zeige RYK Antikörper) 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 (zeige MYOG Antikörper) expression.
Amyloid fibrils formed by a mutant form of TTR, A25T, activate microglia, leading to the secretion of tumor necrosis factor-alpha (TNF-alpha (zeige TNF Antikörper)), interleukin-6 (IL-6 (zeige IL6 Antikörper)) 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 (zeige HP Antikörper), Pig-MAP and monocytes compared to the release of AGP, SAA (zeige SAA1 Antikörper) 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