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Validated All-in-One™ qPCR Primer for TTR(NM_000371.3) Search again
Product ID:
HQP110910
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ATTR, CTS, CTS1, HEL111, HsT2651, PALB, TBPA, TTN
Gene Description:
transthyretin
Target Gene Accession:
NM_000371.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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. [provided by RefSeq].
Gene References into function
- the beta-slip structure and amyloidosis
- structure of a new polymorphic monoclinic form of human transthyretin at 3 A resolution reveals a mixed complex between unliganded and T4-bound tetramers of TTR
- In a model of amyloidogenesis, chemically cross-linked dimeric forms of transthyretin are able to assemble into amyloid fibrils from oligomeric protein building blocks rather than from structurally rearranged monomers.
- incorporation of one or more T119M transthyretin mutant subunits into a predominantly V30M tetramer strongly stabilized the mixed tetramer against dissociation
- Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization
- Structural basis of negative cooperativity in transthyretin
- Transthyretin Val 107 in a Japanese patient with familial amyloid polyneuropathy. point mutation responsible for substitution of valine for isoleucine at position 107
- DNA analysis showed heterozygosity for normal TTR and the amyloidogenic mutation ATTR (Val30Met) leading to the diagnosis of familial amyloidotic polyneuropathy.
- The correlation between destabilization of the transthyretin core strands and the tendency for amyloid formation(familial amyloid polyneuropathy variants) supports the view that these strands are involved in amyloidogenicity
- role in naso-maxillary deformity in transgenic mice
- The amyloidogenic TTR mutant Y114C exists in three forms: one unstable but nativelike tetrameric form, one highly aggregated form in which a network of disulfide bonds is formed, and one fibrillar form.
- Differences in clinical and geographic features between early- and late-onset familial amyloid polyneuropathy TTR Met30 have been confirmed in Japanese patients with onset before and after 50 years of age.
- TTR(105-115) adopts an extended beta-strand conformation that is similar to that found in the native protein except for substantial differences in the vicinity of the proline residue.
- transthyretin amyloidosis inhibitors functioned by increasing the kinetic barrier associated with misfolding, preventing amyloidogenesis by stabilizing the native state; the trans-suppressor mutation also functioned through kinetic stabilization
- The ATTR Val30 Met and ATTR Tyr114Cys mutations induce different clinical features of vitreous opacities
- Transthyretin intronic open reading frames are not independently expressed in vivo or part of functional transcripts.
- In human muscle, the Val122Ile TTR mutation predisposes to A[beta] deposition and amyloidogenesis and increases presumably toxic intracellular A[beta] oligomers.
- an unidirectional dimer to monomer transition of normal TTR is achieved at 70-80 degrees C in neutral to mild alkaline buffers or at 37 degrees C and slightly acidic pH (6-7). Addition of urea favors the transition into monomers.
- novel pathologic TTR variant with an amino acid substitution (Phe->Cys) at position 33; the Cys33 residue was S-sulfonated and S-thiolated (conjugated to cysteine, cysteinylglycine, and glutathione); these adducts may play a role in TTR fibrillogenesis
- consecutive cycles of compression-decompression under aggregating conditions lead to reversible dissociation of transthyretin and alpha-synuclein fibrils
- Wild-type TTR co-deposits in peripheral nerves with variant TTR as amyloid fibril. Progression of amyloid deposition in peripheral nerves from wild-type TTR may occur after liver transplantation, as has been seen in the heart.
- homocysteine and human plasma transthyretin bind and have roles in the pathological consequences of amyloid disease
- TTR dimers containing amyloidogenic TTR mutations decay into monomers at pH<7.4
- a novel transthyretin (TTR) variant, aspartic acid-18 glutamic acid (Glu), causing TTR-related cardiac amyloidosis in a heterozygote
- solvent accessibility analysis of transthyretin amyloid by NMR
- genotype-phenotype correlations in familial amyloid polyneuropathy (V30M) in Portugal and Sweden
- Urea-induced unfolding data indicate that amyloidogenic Tyr114His and Tyr116Ser mutations of transthyretin reduce the stability of its secondary, tertiary, and quaternary structure.
- TTR monomers rapidly aggregate to form transient low molecular mass assemblies that are highly cytotoxic in tissue culture.
- TTR can act as a novel plasma cryptic protease and might have a new, potentially important role under physiological and/or pathological conditions.
- The packing of transthyretin molecules in the C2 crystal form and in the previously determined amyloid TTR (ATTR) Leu55Pro crystal structure is close-to-identical
- mutant TTR may have a role in a severe form of amyloidotic polyneuropathy
- Muscular amyloid angiopathy may contribute to motor nerve injury that, in turn, may lead to amyotropic changes in patients with FAP Ser50Ile and Tyr114Cys.
- Serine112isoleucine variant transthyretin exists as a dimer with nonnative tertiary interactions; it self-assembles under nearly physiological conditions into insoluble spherical aggregates that induce cell death in a human neuroblastoma cell line.
- We report a Chinese patient with amyloidotic polyneuropathy associated with a novel transthyretin mutation (V32A)... likely to be associated with late onset and low-penetrance phenotype.
- biophysical analysis of human transthyretin under partially denaturing conditions
- homozygosity for an amyloidogenic transthyretin mutation may have an effect on phenotype and long term outcome in fatal neuropathic amyloidosis
- An Italian family with TTR arg47 mutation whose members (two women and their father) showed a rapid progression of the peripheral nervous system involvement and died within 5 years of clinical onset.
- A patient with familial amyloid polyneuropathy. Gene analysis revealed a heterozygous Glu54Gly substitution (A-to-G change) in the transthyretin gene.
- Mutataion in the TTR-amyloid fibril protein is associated with familial amyloid polyneuropathy
- Protein synthesis, including TTR, was reduced in old sheep CP and in newly secreted CSF. These age-related changes suggest reduced capacity of CP to maintain CSF T4 homeostasis and be an added risk for Alzheimer's disease.
- TTR can bind to the plasma membrane and cause a change in membrane fluidity which may be the cause of neurotoxicity.
- Present in all the eye structures except the lens and tear. Significant decrease in vitreous TTR in diabetes with hypertension and increase in one case each of diabetes with hypertension associated with leukaemia or carcinoma with hepato-splenomegaly.
- All three major serum-binding proteins, thyroxine-binding globulin, transthyretin, and albumin, were present in cytosol. May modify thyroid hormone deiodination and materno-fetal thyroid hormone transport.
- results suggest that an intermolecular cysteine bridge at position 114 enhances the exposure of cysteine 10, thereby facilitating additional intermolecular cysteine assemblies
- A Swedish family is reported with rare Phe33Leu transthyretin mutation; the phenotype is characterized by familial amyloidotic polyneuropathy and carpal tunnel syndrome.
- crystal structure of the complex of human transthyretin (hTTR) with 3,3',5,5'-tetraiodothyroacetic acid (T4Ac) determined to 2.2 Angstrom resolution
- analysis of role of dimerization in transthyretin amyloidosis
- We have identified an siRNA that specifically inhibits mutant, but not wild-type, TTR expression even in cells expressing both alleles.
- Data show that chromium(III) and thyroxine cooperatively suppress in vitro fibril formation due to the stabilization of WT-transthyretin (TTR) and V30M-TTR.
- Serotonergic hypofunction in depression, reflected by low CSF 5-HIAA, may result in decreased choroid plexus transthyretin production, alterations in central thyroid hormone kinetics, and increased vulnerability to suicidal ideation and perhaps suicide
- First report describing the presence of differential post-translational oxidations of transthyretin in the cerebral spinal fluid of patients with Alzheimer's disease.
- Transthyretin is clearly not produced in the brain parenchyma of wild-type mice nor in transgenic mouse models of Alzheimer's disease.
- data does not support an involvement of the TTR gene in the pathophysiology of schizophrenia
- C-terminal fragment of the TTR polypeptide chain seems to be crucial for production of abnormal fibrils.
- show involvement of ER stress response in familial amyloid polyneuropathy by showing activation of classical unfolded protein response pathways in tissues not specialized in TTR synthesis but presenting extracellular TTR aggregate and fibril deposition.
- The unstructured N-terminal region of TTR critically influences the specificity and affinity of thyroid hormone binding to TTR.
- The finding of a structural difference between wildtype ATTR and ATTR V30M material on one hand and ATTR Y114C material on the other suggests that the fibril formation pathway of these ATTR variants may differ in vivo.
- In amyloidosis, deposits in both vitreous and cardiac tissues were enriched in variant transthyretin, vitreous fibrils contained more variant protein than cardiac fibrils.
- the effect of oxidation on transthyretin was investigated by comparing the kinetics of fibril formation.
- Destabilization of the dimer-dimer interface and the monomer core is important for the amyloidogenesis of transthyretin.
- Transthyretin preferentially binds to aggregated rather than monomeric beta-amyloid and arrests further growth of the aggregates.
- The asymmetry and a possible destabilization of the tetrameric quaternary structure of TTR may be responsible for the amyloidogenic potential of the two TTR mutant forms at low pH.
- results show that transthyretin is present in amniotic fluid of preeclamptic & control women as a mixture of dimeric & post-translationally modified monomeric forms; preeclamptic women showed a significant increase in the amount of monomeric proteins
- assays for TTR have a relatively high level of uncertainty; clinical evaluation--history and physical examination--should remain the mainstay of nutritional assessment.
- Endoplasmic reticulum quality control regulates the fate of TTR variants in the cell.
- Thus, there was considerable phenotypic heterogeneity among family members with FAP despite the identical TTR genotype.
- These results suggest that oxidative stress to cells abrogates secretion of DJ-1 and that secreted DJ-1 degrades aggregated TTR to protect against the onset of FAP.
- study of 49 TTR mutations including 33 resulting in electrically neutral amino acid substitutions; most of the electrically neutral amyloidogenic TTR variants had in common a reduced conformational stability of monomers by the activity of protons & urea
- Transthyretin mutation is associated with vitreous amyloid
- present two families, from Spain and Portugal, with familial amyloid polyneuropathy (FAP) associated with the mutation TTRSer50Arg
- Data show that Cu(II) and Zn(II) promoted amyloid formation from the L55P mutant of transthyretin at pH 6.5.
- Extended high-temperature incubation of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S successfully removes heterogeneities and allows the reproducible growth of well diffracting crystals.
- proposed for TTR fibrillogenesis inhibitor screens avoids not only lengthy and cumbersome large-scale protein isolation steps but also artefacts associated with most current in vitro first-line screening methods
- Reduced transthyretin expression is associated with lung cancer
- DNA testing for transthyretin is the most reliable test for transthyretin familial amyloid polyneuropathy in patients with a progressive length-dependent small fiber polyneuropathy of unknown origin, especially when associated with autonomic dysfunction.
- First described case of a TTR-Phenylalanine-64-serine mutation in an African-American family with profound gastrointestinal symptoms.
- Serum RBP4 and TTR showed no differences between controls/type 1 diabetic children.
- Data are consistent with the continued deposition of normal transthyretin in cardiac tissue after liver transplantation.
- Report identified a novel TTR Gly67Glu mutant and it was the first case series of familial transthyretin amyloidosis.
- Elevated IOP (intraocular pressure) may develop in patients with vitreous amyloidosis due to a TTR Val30Gly mutation in the transthyretin gene.
- Our study is the first case series gathering from the Chinese-Taiwanese population. We proposed a possible hot-spot mutation of the TTR gene, Ala97Ser, in this ethnic group.
- a novel post-translational modification, gamma-carboxylation of the Glu-42 (Gla-42), of transthyretin was observed in moyamoya disease
- TTR-MT1/2 complexes may be functionally significant not only in healthy conditions but also in Abeta deposition in Alzheimer disease.
- In patients with renal disease, serum transthyretin is positively and independently related to body mass index and is significantly lower in malnourished than well-nourished patients.
- Serum transthyretin concentrations are not related to birth weight/gestational age and are not associated with either clinical condition at birth (as assessed by Apgar score) or the occurrence of respiratory distress syndrome.
- Upregulation of transthyretin is associated with brain metastases in lung cancer
- transthyretin down-regulation may have a role in cholangiocarcinoma
- conformational changes preceding the formation of amyloid, we performed molecular dynamics simulations of the wild-type monomer, amyloidogenic variants of transthyretin (V30M, L55P, V122I) and a protective variant (T119M) at neutral and low pH
- Fluorescence-detected sedimentation velocity was used to determine the effect of S-sulfonate and S-cysteine on the quaternary structural stability of fluorophore-conjugated recombinant TTR.
- TTR mRNA expression in caudate equina, dorsal root ganglia, frontal lobe.
- FAP with TTR Val30Met mutation in Japan can be classified to (i) early-onset and endemic (Nagano and Kumamoto), (ii) late-onset and endemic (Ishikawa), and (iii) late-onset and non-endemic types.
- Quantifying the transthyretin/prostaglandin-D-synthase complex in ventricular cerebrospinal fluid may be useful in the diagnosis of Alzheimer disease, possibly in its early stages.
- The origin of the the TTR Val30Met familial amyloid polyneuropathy mutation arose independently in Portugal and in Sweden, and spread out from Portugal to Brazil.
- novel Thr49Pro TTR gene mutation is associated with leptomeningeal amyloidosis resulting in recurrent CNS symptoms
- TTR identified patients at highest risk for metabolic losses associated with stress hypermetabolism.
- acidic conditions increase the susceptibility of the EF helix-loop of the B subunit to undergo conformational changes and unfold, destabilizing the tetramer and identifying conformational changes in the tetramer that lead to the amyloidogenic monomer
- The aqueous humor of glaucoma patients revealed characteristic differences in protein/peptide profiles from control patients using two different analytical methods, SELDI-TOF-MS and two-dimensional electrophoresis.
- DNA testing for transthyretin is the most reliable test for transthyretin familial amyloid polyneuropathy in patient of Russian family.
- Its dynamic structure changes due to pathogenic mutation and accumulates in various organs to cause amyloidosis. (review)
- Islets of Langerhans expression of transthyretin may be altered in type-2 diabetes.
- TTR deposited in peripheral nervous system of familial amyloiditic polyneuropathy should be regarded as having blood or CSF orgin
- TTR Val30Met mutation is associated with familial amyloid polyneuropathy.
- A 33-year-old man with FAP type I with genetic findings of transthyretin (TTR) revealed G to A transition in codon 54 causing a rare mutation of TTR Lys54.
- The protein-protein interactions between transthyretin and plasma retinol-binding protein were analysed by structural (X-ray crystallography) and genetic (amino acid substitutions) methods.
- The results show a higher proportion of wtTTR in the 12-months-surviving amyloidosis patient than the 3-weeks-surviving patient, but interestingly this difference in wt proportion is mainly seen among the full-length, and not the fragmented, molecules.