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The protein encoded by TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is located on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Additionally we are shipping Cardiac Troponin T2 Kits (72) and Cardiac Troponin T2 Proteins (36) and many more products for this protein.
Showing 10 out of 381 products:
Human Polyclonal Cardiac Troponin T2 Primary Antibody for EIA, WB - ABIN951043
Millat, Chanavat, Créhalet, Rousson: Development of a high resolution melting method for the detection of genetic variations in hypertrophic cardiomyopathy. in Clinica chimica acta; international journal of clinical chemistry 2010
Show all 3 references for 951043
Cow (Bovine) Polyclonal Cardiac Troponin T2 Primary Antibody for WB - ABIN2776953
Klaassen, Probst, Oechslin, Gerull, Krings, Schuler, Greutmann, Hürlimann, Yegitbasi, Pons, Gramlich, Drenckhahn, Heuser, Berger, Jenni, Thierfelder: Mutations in sarcomere protein genes in left ventricular noncompaction. in Circulation 2008
Chicken Monoclonal Cardiac Troponin T2 Primary Antibody for IF, IHC (p) - ABIN180606
Malouf, McMahon, Oakeley, Anderson: A cardiac troponin T epitope conserved across phyla. in The Journal of biological chemistry 1992
Human Monoclonal Cardiac Troponin T2 Primary Antibody for EIA, FACS - ABIN1105666
Hershberger, Pinto, Parks, Kushner, Li, Ludwigsen, Cowan, Morales, Parvatiyar, Potter: Clinical and functional characterization of TNNT2 mutations identified in patients with dilated cardiomyopathy. in Circulation. Cardiovascular genetics 2009
Human Monoclonal Cardiac Troponin T2 Primary Antibody for IA, WB - ABIN265695
Qiao, Tang, Munske, Dutta, Ivory, Dong: Enhanced fluorescence anisotropy assay for human cardiac troponin I and T detection. in Journal of fluorescence 2011
Higher postoperative concentrations of high-sensitivity troponin T are independently associated with all-cause mortality in patients undergoing on-pump cardiac surgery.
variants in TNNT2 and BAG3 (show BAG3 Antibodies) are associated with a high propensity to life-threatening cardiomyopathy presenting from childhood and young adulthood.
Binding of the MBNL (show MBNL1 Antibodies) zinc fingers to cardiac troponin T pre-mRNA is specific and relatively simple, unlike the complex multiple dimer-trimer stoichiometries postulated in some previous studies.
The measurement of high-sensitivity cardiac troponin T plasma concentration within large nationally-representative surveys such as the Health Survey for England is feasible.
Data suggest that modulation of structural dynamics far from the regulatory Ca2 (show CA2 Antibodies)+-binding site is the underlying molecular mechanism for many TNNC1 (show TNNC1 Antibodies) mutations in patients with hypertrophic cardiomyopathies or familial hypertrophic cardiomyopathies; many mutations affect balance between open and closed conformations; troponin I switch peptide [TnI (show TNNI2 Antibodies)(SW)] switch peptide binds to TNNC1 (show TNNC1 Antibodies) and stabilizes the open TNNC1 (show TNNC1 Antibodies) conformation.
Data suggest that the tropomyosin (show TPM2 Antibodies) overlap region structure and function are affected differentially by a point mutation in cardiac tropomyosin (TPM1, D230N) that is associated with dilated cardiomyopathy as compared to a point mutation in cardiac troponin T (TNNT2, R92L) that is associated with hypertrophic cardiomyopathy.
High T2-weighted signal intensity on cine MRI is associated with elevated troponin T in hypertrophic cardiomyopathy.
The high negative predictive value of preoperative hs-cTnT and NT-proBNP suggest usefulness as a "rule-out" test to confirm low risk of postoperative Myocardial Infarction
Generated is a gene-targeted knock-in murine model of the autosomal dominant Arg141Trp (R141W) mutation in human Tnnt2. Tnnt2 R141W mutation causes a Ca2 (show CA2 Antibodies)+ desensitization and mice adapt by increasing Ca2 (show CA2 Antibodies)+-transient amplitudes, which impairs Ca2 (show CA2 Antibodies)+ handling dynamics, metabolism and responses to beta-adrenergic activation.
A myosin activator improves actin assembly and sarcomere function of human-induced pluripotent stem cell-derived cardiomyocytes with a troponin T point mutation.
We show that the phosphorylation of cTnI and alphaTm vary in the different chambers of the heart, whereas the phosphorylation of MLC2 and cTnT does not.
Significant changes in thin filament Ca2 (show CA2 Antibodies)+-sensitivity, structure and kinetics are brought about through PKC (show PKC Antibodies) phosphorylation of cardiac troponin T.
The mu-calpain-mediated proteolytic modification of TnT by removing the NH2-terminal variable region of TnT may act as an acute mechanism to adjust muscle contractility under stress conditions.
Substituting smooth muscle caldesmon for skeletal muscle troponin produces a similar decrease and re-increase in fluorescence, but the apparent rate constant for the increase is >10 times that observed with troponin.
In ischemic myocardium, the expression of cTnT showed prominent focal or flaky depletion in myocardial cytoplasm with no expression detected in interstitium.
TnTA30V mutation attenuated Ca(2 (show CA2 Antibodies)+)-activated maximal tension and length-mediated cross-bridge recruitment against alpha-myosin (show MYH6 Antibodies) heavy chain but augmented these parameters against beta-myosin heavy chain (show MYH7 Antibodies), suggesting divergent contractile phenotypes.
The shift from cTnT exon 5 inclusion to exclusion during development was delayed in the heart of Ts65Dn mice due to Dyrk1A (show DYRK1A Antibodies) overexpression.
for hypertrophic cardiomyopathy (HCM)-causing mutations in TnT (show TNNI1 Antibodies), Ca(2 (show CA2 Antibodies)+)-sensitisation together with uncoupling in vitro is the usual response and both factors may contribute to the HCM phenotype
cardiomyopathy mutation (R97L) in mouse cardiac troponin T has an effect on the muscle length-mediated recruitment of crossbridges and is modified divergently by alpha- and beta-myosin heavy chain (show MYH7 Antibodies)
Data indicate that high-sensitivity troponin T (hs-TnT) levels are influenced by myocardial dysfunction/heart failure (HF) in acute exacerbation of chronic obstructive lung disease (AECOPD), but provide independent prognostic information.
cTnT elevation emerged as a strong, independent predictor of 30-day mortality and remained a modest, but significant, predictor throughout 2 years post transcatheter aortic valve implantation.
MBPC and troponin-I phosphorylation modulate myofilament length-dependent activation
Data indicate that the troponin T Tnnt2(MerCreMer/+) mouse model also provides a useful tool to trace myocardial lineage during development.
TnT (show TNNI1 Antibodies) mutation F72L leads to contractile changes that are linked to dilated cardiomyopathy in the presence of MYH6 (show MYH6 Antibodies) and hypertrophic cardiomyopathy in the presence of MYH7 (show MYH7 Antibodies).
TNT increases slightly during low flux-hemodialysis. High-flux hemodialysis eliminates the biomarker and can mask increases caused by cardiac disease.
Data showed that CXCR4a was significantly more highly expressed in tnnt2 knocked down mutant at 48 and 60 hpf than controls.
We show that the zebrafish silent heart (sih) mutation affects the gene tnnt2.
Tnnt1 (show TNNI1 Antibodies), Tnnt2, and Tnnt3b were conserved in the central tropomyosin (show TPM2 Antibodies)- and C-terminal troponin I-binding domains but the N-terminal hypervariable regions were highly extended and rich in glutamic acid in polypeptides of Tnnt1 (show TNNI1 Antibodies) and Tnnt2, but not Tnnt3b.
The protein encoded by this gene is the tropomyosin-binding subunit of the troponin complex, which is located on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in this gene have been associated with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy. Transcripts for this gene undergo alternative splicing that results in many tissue-specific isoforms, however, the full-length nature of some of these variants has not yet been determined.
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