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TTR encodes transthyretin, one of the three prealbumins including alpha-1-antitrypsin, transthyretin and orosomucoid. Additionally we are shipping Transthyretin Kits (85) and Transthyretin Proteins (76) and many more products for this protein.
Showing 10 out of 308 products:
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 references for ABIN1585446
Human Polyclonal TTR Primary Antibody for FACS, IHC (p) - ABIN390652
Lee, Lee, Son, Kim, Park, Roh, Kim, Kang, Cho, Choi: Clusterin regulates transthyretin amyloidosis. in Biochemical and biophysical research communications 2009
Mouse (Murine) Polyclonal TTR Primary Antibody for ICC, IHC (fro) - 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, WB - ABIN185630
Sekijima, Wiseman, Matteson, Hammarström, Miller, Sawkar, Balch, Kelly: The biological and chemical basis for tissue-selective amyloid disease. in Cell 2005
Human Monoclonal TTR Primary Antibody for EIA, WB - ABIN492376
Olsson, Norgren, Obayashi, Plante-Bordeneuve, Suhr, Cederquist, Jonasson: A possible role for miRNA silencing in disease phenotype variation in Swedish transthyretin V30M carriers. in BMC medical genetics 2010
Data suggest that well-structured AB loop regions of TTR in native/homotetrameric/stable state become dissociated/disordered/unfolded at low pH; during refolding, structural perturbations in AB loop appear and facilitate misfolding and amyloid formation.
Study elucidated alterations in TTR, APP (show APP Antibodies) and the global gene expression profile in the frontal cortex between idiopathic normal pressure hydrocephalus patients and nondemented control brain
Quantitative analysis of post-translational modifications in human serum transthyretin associated with familial amyloidotic polyneuropathy by targeted LC-MS and intact protein MS.
Large differences in survival were observed in hereditary transthyretin amyloidosis patients with TTR mutations other than Val30Met.
Ile107Val and LateMet30 TTR mutations are associated with the most debilitating and severe familial amyloid polyneuropathy, with rapid onset of tetraparesis and shorter median survival.
study reports a novel TTR variant(TTR Asp38Tyr mutation) in 2 Brazilian sisters who developed a late onset neuropathy; new mutation calls attention to the diversity found in TTR familial amyloid polyneuropathy
The structures of TTR in complex with three natural polyphenols (pterostilbene, quercetin and apigenin) have been determined.
beta-strands F and H as necessary for TTR aggregation.
Given the high conservation of TTR structure, function and tissue specificity and timing of gene expression, this implies that TTR has a fundamental role, during development and in the adult.
Open-label clinical trial of tafamidis in patients with non-Val30Met and non-Val122Ile hereditary transthyretin amyloidosis shows no change in cardiac findings.
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.
Hsf-1 (show HSF1 Antibodies) affects podocyte markers NPHS1 (show NPHS1 Antibodies), NPHS2 and WT1 (show WT1 Antibodies) in a transgenic mouse model of TTRVal30Met-related amyloidosis.
Fibroblasts endocytose and degrade transthyretin aggregates in transthyretin-related amyloidosis.
Increased degradation of 14-3-3zeta (show YWHAZ Antibodies) in lysosomes in the absence of TTR, increasing autophagy.
our data demonstrate that the increased expression of Ttr in ob/ob mice does not cause (but rather attenuates) their phenotypic abnormalities.
TTR has an important and nonredundant role in influencing the development of several organs.
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