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TTN encodes a large abundant protein of striated muscle. De plus, nous expédions Titin Anticorps (57) et Titin Protéines (6) et beaucoup plus de produits pour cette protéine.
Showing 9 out of 21 products:
Human Titin Kit ELISA pour Sandwich ELISA - ABIN414785
Li, Li, Wang, Yang: Proteomic analysis of effluents from perfused human heart for transplantation: identification of potential biomarkers for ischemic heart damage. dans Proteome science 2012
The T-allele at rs10497520 in the TTN gene is associated with shorter skeletal muscle fascicle length and conveys an advantage for marathon running performance in habitually trained men.
An overview of the different neuromuscular disorders caused by mutations in the TTN gene, reviewing the molecular findings as well as the clinical data (review).
This review considers data on structural and functional features of titin, on the role of this protein in determination of mechanical properties of sarcomeres, and on specific features of regulation of the stiffness and elasticity of its molecules, and possible amyloid aggregation of this protein
Exome sequencing was conducted and a novel mutation c.107788T>C (p.W35930R) in the titin gene (TTN) was identified.
Study found that there is a missense mutation in the TTN gene, c.100126A > G (p.Thr33376Ala), in a family whose members suffer from familial dilated cardiomyopathy. TTN is closely related to dilated cardiomyopathy and is an important causative gene of familial dilated cardiomyopathy.
Truncating titin mutations cause a mild and treatable form of dilated cardiomyopathy.
Activation of titin protein represents an initial step forward adaptive remodelling of the exercised muscle and may also be involved in the initiation of myofibre repair.
Novel A178D missense mutation in titin is a cause of a highly penetrant familial cardiomyopathy with features of left ventricular noncompaction.
Quantitative models derived from large-scale human genetic and phenotypic data can be applied to truncating mutations in titin in dilated cardiomyopathy.
Variants near TTN and CCDC8 (Montrer CCDC8 Kits ELISA) were associated with KI67 (Montrer MKI67 Kits ELISA) expression, and rs2288563 and rs2562832 in TTN are potential biomarkers for the prediction of clinical outcomes in hepatitis B-related hepatocellular carcinoma patients.
regulation of thick filament length depends on titin and is critical for maintaining muscle health.
It is likely that titin plays a role in the increase of active muscle stiffness during rapid unloading. These results are consistent with the idea that, in addition to the thin filaments, titin is activated upon Ca(2 (Montrer CA2 Kits ELISA)+) influx in skeletal muscle.
Titin-based force enhancement in skeletal muscle is essentially absent in muscular dystrophy with myositis sarcomeres where amino acids in N2A and PEVK titin are deleted, indicating these specific regions along titin are paramount in increasing titin stiffness in an active sarcomere.
Our data suggest that Tbeta4 is required for setting correct sarcomere length and for appropriate splicing of titin, not only in the heart but also in skeletal muscle.
Phosphorylating Titin's Cardiac N2B Element by ERK2 (Montrer MAPK1 Kits ELISA) or CaMKIIdelta Lowers the Single Molecule and Cardiac Muscle Force
Cleavage of C-terminal titin by CAPN3 (Montrer CAPN3 Kits ELISA) is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy.
titin affects the tuning of shivering frequency
An increase in the degree of titin phosphorylation results in increased proteolytic degradation of this protein, that contributes to the development of skeletal muscle atrophy.
Pure volume overload induces an increase in titin stiffness that is beneficial and limits eccentric remodeling.
increased titin stiffness promotes myocardial contraction by accelerating the formation of force-generating cross-bridges without decelerating relaxation
titin may be a factor involved in the Frank-Starling mechanism of the heart by promoting actomyosin interaction in response to stretch
calcium affects passive myocardial tension in a titin isoform-dependent manner.
Upon relaxation of shortened myocytes, the restoring stiffness correlates with the titin isoform expression profile with myocytes that express high levels of the stiff isoform (N2B) having the highest restoring stiffness.
Data show that disulfide isomerization reactions within Ig domains enable a third mechanism of titin elasticity.
A dual-beam optical tweezers measured the mechanics of human alpha-actinin 2 (Montrer ACTN2 Kits ELISA) and titin interaction at the single-molecule level. Depending on the direction of force application, the unbinding forces can more than triple. Multiple alpha-actinin (Montrer ACTN1 Kits ELISA)/Z-repeat interactions cooperate to ensure long-term stable titin anchoring, while allowing the individual components to exchange dynamically.
The results of this study are consistent with the claim that residual force enhancement is present and is regulated by titin in skeletal psoas myofibrils, but not cardiac papillary myofibrils
landscape recovered all features of our nanomechanics results. The ensemble molten-globule dynamics delivers significant added contractility that may assist sarcomere mechanics, and it may reduce the dissipative energy loss associated with titin unfolding/refolding during muscle contraction/relaxation cycles.
Work done by titin protein folding assists muscle contraction.
Suggest that the increase in the static tension in activated striated muscle is directly associated with Ca(2+)-dependent change in titin properties and not associated with changes in titin-actin interactions.
titin's visco-elastic properties appear to depend on the Ig do- main un/refolding kinetics and that indeed, titin (and thus myofibrils) can become virtually elastic when Ig domain un/refolding is prevented.
Under non-equilibrium conditions across the physiological force range, titin extends by a complex pattern of history-dependent discrete conformational transitions.
We tested the hypothesis that titin properties might be reflected well in single myofibrils. mechanics of titin are well preserved in isolated myofibrils.
Titin might be responsible for passive force enhancement observed in myofibrils.
Two polymorphisms previously identified and described in the 3'UTR (Montrer UTS2R Kits ELISA) of MYPN (Montrer MYPN Kits ELISA) and TTN genes in a group of Italian Large White (ILW) and Italian Duroc (ID) pigs, were analysed.
Titin-actin interaction: PEVK-actin-based viscosity in a large animal.
Neonatal pig hearts showed large N2BA-titin isoforms distinct from those present in the adult porcine myocardium.
findings demonstrate that Tn plays an important role in the Frank-Starling mechanism of the heart via on-off switching of the thin filament state, in concert with titin-based regulation
Report PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness.
Coexpression of the 2 titin isoforms in large mammals allows longer sarcomere lengths without the development of excessive diastolic tension.
This gene encodes a large abundant protein of striated muscle. The product of this gene is divided into two regions, a N-terminal I-band and a C-terminal A-band. The I-band, which is the elastic part of the molecule, contains two regions of tandem immunoglobulin domains on either side of a PEVK region that is rich in proline, glutamate, valine and lysine. The A-band, which is thought to act as a protein-ruler, contains a mixture of immunoglobulin and fibronectin repeats, and possesses kinase activity. An N-terminal Z-disc region and a C-terminal M-line region bind to the Z-line and M-line of the sarcomere, respectively, so that a single titin molecule spans half the length of a sarcomere. Titin also contains binding sites for muscle associated proteins so it serves as an adhesion template for the assembly of contractile machinery in muscle cells. It has also been identified as a structural protein for chromosomes. Alternative splicing of this gene results in multiple transcript variants. Considerable variability exists in the I-band, the M-line and the Z-disc regions of titin. Variability in the I-band region contributes to the differences in elasticity of different titin isoforms and, therefore, to the differences in elasticity of different muscle types. Mutations in this gene are associated with familial hypertrophic cardiomyopathy 9, and autoantibodies to titin are produced in patients with the autoimmune disease scleroderma.
, rhabdomyosarcoma antigen MU-RMS-40.14
, titin protein homolog