Titin Proteine (TTN)

TTN encodes a large abundant protein of striated muscle. Zusätzlich bieten wir Ihnen Titin Antikörper (57) und Titin Kits (20) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
TTN 7273 Q8WZ42
Maus TTN TTN 22138  
Ratte TTN TTN 84015  
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Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
Escherichia coli (E. coli) Human His tag   50 μg Anmelden zum Anzeigen 11 Days
Escherichia coli (E. coli) Human His tag 100 μg Anmelden zum Anzeigen 15 bis 18 Tage
Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 11 bis 12 Tage
Escherichia coli (E. coli) Human Unkonjugiert   100 μg Anmelden zum Anzeigen 11 bis 18 Tage

TTN Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human ,

Weitere Proteine zu Titin (TTN) Interaktionspartnern

Human Titin (TTN) Interaktionspartner

  1. Truncating titin mutations cause a mild and treatable form of dilated cardiomyopathy.

  2. 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.

  3. Novel A178D missense mutation in titin is a cause of a highly penetrant familial cardiomyopathy with features of left ventricular noncompaction.

  4. Quantitative models derived from large-scale human genetic and phenotypic data can be applied to truncating mutations in titin in dilated cardiomyopathy.

  5. Variants near TTN and CCDC8 (zeige CCDC8 Proteine) were associated with KI67 (zeige MKI67 Proteine) expression, and rs2288563 and rs2562832 in TTN are potential biomarkers for the prediction of clinical outcomes in hepatitis B-related hepatocellular carcinoma patients.

  6. Recent studies classify pathogenic variants in the TTN gene as the main responsible for Familial Dilated Cardiomyopathy.

  7. Heterozygous loss of RBM20 (zeige RBM20 Proteine) suffices to profoundly impair myocyte biomechanics by its disturbance of TTN splicing causing dilated cardiomyopathy.

  8. Study identified a probable association between variation in TTN gene and patients with sudden unexpected death syndrome.

  9. We report that missense variant in the A-band of TTN gene is the strongest candidate mutation for autosomal-dominant inguinal hernia with incomplete penetrance.

  10. Titin-truncating variant is associated with dilated cardiomyopathy.

Mouse (Murine) Titin (TTN) Interaktionspartner

  1. 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 (zeige CA2 Proteine)+) influx in skeletal muscle.

  2. 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.

  3. 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.

  4. Phosphorylating Titin's Cardiac N2B Element by ERK2 (zeige MAPK1 Proteine) or CaMKIIdelta Lowers the Single Molecule and Cardiac Muscle Force

  5. Cleavage of C-terminal titin by CAPN3 (zeige CAPN3 Proteine) is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy.

  6. titin affects the tuning of shivering frequency

  7. 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.

  8. Pure volume overload induces an increase in titin stiffness that is beneficial and limits eccentric remodeling.

  9. increased titin stiffness promotes myocardial contraction by accelerating the formation of force-generating cross-bridges without decelerating relaxation

  10. alpha-Synemin (zeige SYNM Proteine) localizes to the M-band of the sarcomere through interaction with the M10 region of titin

Fruit Fly (Drosophila melanogaster) Titin (TTN) Interaktionspartner

  1. Here we show using Drosophila indirect flight muscle that the filamin ortholog Cheerio in conjunction with the giant elastic protein titin plays a crucial role in keeping thin filaments stably anchored at the Z-disc. We identify the filamin domains required for interaction with the titin ortholog Sallimus, and we demonstrate a genetic interaction of filamin with titin and actin.

  2. Sls is a novel hub gene responsible for the regulation of mitochondrial respiration in the muscle sarcomere.

  3. Projectin immunolocalization studies during myofibrillogenesis in Drosophila indirect flight muscles.

  4. Projectin is oriented within the indirect flight muscles sarcomere with its NH2-terminus embedded in the Z-bands. This protein has an elastic region, possibly the PEVK-like domain located close to the NH2-terminus.

  5. Alternative Sls isoforms could regulate the stiffness of the many fibre types in Drosophila muscles.

  6. Results reveal a role for Mlp84B in maintaining muscle structural integrity, and suggest Mlp84B and D-titin cooperate to stabilize muscle sarcomeres.

Cow (Bovine) Titin (TTN) Interaktionspartner

  1. titin may be a factor involved in the Frank-Starling mechanism of the heart by promoting actomyosin interaction in response to stretch

  2. calcium affects passive myocardial tension in a titin isoform-dependent manner.

  3. 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.

Rabbit Titin (TTN) Interaktionspartner

  1. 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

  2. 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.

  3. Work done by titin protein folding assists muscle contraction.

  4. 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.

  5. 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.

  6. Under non-equilibrium conditions across the physiological force range, titin extends by a complex pattern of history-dependent discrete conformational transitions.

  7. We tested the hypothesis that titin properties might be reflected well in single myofibrils. mechanics of titin are well preserved in isolated myofibrils.

  8. Titin might be responsible for passive force enhancement observed in myofibrils.

  9. The structure and self-interactive properties of an approximately 290 kDa ( approximately 100 nm long) tryptic fragment from the I-band part of titin that is extensible in situ, is presented.

  10. results suggest residual force enhancement in skeletal muscle fibers is caused by stiffening of titin upon muscle activation but not with titin binding to actin; finding indicates existence of a Ca(2 (zeige CA2 Proteine)+)-regulated, titin-based stiffness in skeletal muscle

Pig (Porcine) Titin (TTN) Interaktionspartner

  1. Two polymorphisms previously identified and described in the 3'UTR of MYPN (zeige MYPN Proteine) and TTN genes in a group of Italian Large White (ILW) and Italian Duroc (ID) pigs, were analysed.

  2. Titin-actin interaction: PEVK-actin-based viscosity in a large animal.

  3. Neonatal pig hearts showed large N2BA-titin isoforms distinct from those present in the adult porcine myocardium.

  4. 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

  5. Report PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness.

  6. Coexpression of the 2 titin isoforms in large mammals allows longer sarcomere lengths without the development of excessive diastolic tension.

Titin (TTN) Protein Überblick

Protein Überblick

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.

Genbezeichner und Symbole assoziert mit Titin Proteine (TTN)

  • titin (TTN)
  • titin (Ttn)
  • bent (bt)
  • sallimus (sls)
  • titin (titin)
  • titin (TTNLOC100620261)
  • 0020/01 Protein
  • 39c-18 Protein
  • 1100001C23Rik Protein
  • 2310036G12Rik Protein
  • 2310057K23Rik Protein
  • 2310074I15Rik Protein
  • AF006999 Protein
  • anon-CREST Protein
  • AV006427 Protein
  • Bt Protein
  • CG1479 Protein
  • CG1915 Protein
  • CG10285 Protein
  • CG18242 Protein
  • CG18245 Protein
  • CG18857 Protein
  • CG32019 Protein
  • CMD1G Protein
  • CMH9 Protein
  • CMPD4 Protein
  • CT3598 Protein
  • CT8086 Protein
  • CT41299 Protein
  • d-titin Protein
  • D330041I19Rik Protein
  • D830007G01Rik Protein
  • Dmel\\CG1915 Protein
  • Dmel\\CG32019 Protein
  • EOMFC Protein
  • HMERF Protein
  • ket Protein
  • kettin Protein
  • KZ Protein
  • l(2)2 Protein
  • l(2)23 Protein
  • l(3)62Ca Protein
  • l(3)Ca Protein
  • l(3)dre8 Protein
  • l(3)j1D7 Protein
  • l(3)rL182 Protein
  • l(3)S002001 Protein
  • l(4)2 Protein
  • l(4)21 Protein
  • l(4)23 Protein
  • l(4)37 Protein
  • l(4)38 Protein
  • l(4)102CDa Protein
  • l(4)PT-2 Protein
  • L56 Protein
  • LGMD2J Protein
  • MCP Protein
  • mdm Protein
  • MYLK5 Protein
  • Prj Protein
  • sal Protein
  • sam Protein
  • shru Protein
  • Sls Protein
  • Titin Protein
  • TMD Protein
  • UNC-22 Protein

Bezeichner auf Proteinebene für Titin Proteine (TTN)

connectin , rhabdomyosarcoma antigen MU-RMS-40.14 , C-protein , CG32019-PC , CG32019-PF , CG32019-PH , CG32019-PI , bt-PC , bt-PF , bt-PH , bt-PI , lethal(4) Powell, Tennessee-2 , myosin LCK , projectin , projectin myosin light chain kinase , twitchin , CG1915-PA , CG1915-PD , CG1915-PP , CG1915-PQ , CG1915-PR , CG1915-PS , CG1915-PT , CG1915-PU , CG1915-PV , CG1915-PW , CG1915-PX , CG1915-PY , CG1915-PZ , D-titin , D-titin-KZ , dtitin , kettin , lethal (3) S002001 , lethal(3)62Ca , mitotic chromosomal protein , salimus , sls-PA , sls-PD , sls-PP , sls-PQ , sls-PR , sls-PS , sls-PT , sls-PU , sls-PV , sls-PW , sls-PX , sls-PY , sls-PZ , titin , titin protein homolog

7273 Homo sapiens
22138 Mus musculus
43814 Drosophila melanogaster
44013 Drosophila melanogaster
84015 Rattus norvegicus
424126 Gallus gallus
540561 Bos taurus
1791505 Rhodopirellula baltica SH 1
100008570 Oryctolagus cuniculus
100620261 Sus scrofa
100722767 Cavia porcellus
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