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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
Show all 4 Pubmed References
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 ELISA - ABIN2481284
Beetham, Dawnay, Ghany, Dubrey, Miles: A radioimmunoassay for human urinary prealbumin. in Annals of clinical biochemistry 1993
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
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
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
we identify a somatic mosaicism, in several subjects affected by familial amyloidotic polyneuropathy, involving the dominant c.325G>C mutation of the TTR gene
The role of Transthyretin in the regulation of Ubc9 (show UBE2I Antibodies) SUMOylation
Gene sequencing revealed a phenylalanine-->isoleucine mutation in the 33rd position of exon 2 of TTR in 1 patient of 1 pedigree, confirming the diagnosis of FAP. Two patients subsequently were found to have sensorimotor autonomic neuropathy, whereas 2 others had subclinical autonomic dysfunction.
TTR V30M aggregates and autophagy impairment are associated with Transthyretin amyloidoses .
In Afro-Caribbean patients living in London, ATTR V122I is an underappreciated cause of heart failure, and cardiomyopathy is often misattributed to hypertension.
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.
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.
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