Titin (TTN) ELISA Kits

TTN encodes a large abundant protein of striated muscle. Zusätzlich bieten wir Ihnen Titin Antikörper (55) und Titin Proteine (9) und viele weitere Produktgruppen zu diesem Protein an.

list all ELISA KIts Gen GeneID UniProt
TTN 7273 Q8WZ42
Anti-Ratte TTN TTN 84015  
TTN 22138  
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Top Titin ELISA Kits auf antikoerper-online.de

Showing 9 out of 19 products:

Katalog Nr. Reaktivität Sensitivität Bereich Bilder Menge Anbieter Lieferzeit Preis Details
Human 0.113 ng/mL 0.31-20 ng/mL 96 Tests Anmelden zum Anzeigen 11 bis 15 Tage
562,96 €
Details
Human 0.78 1.56   96 Tests Anmelden zum Anzeigen 6 bis 8 Tage
653,71 €
Details
Meerschweinchen 0.469 ng/mL 0.781-50 ng/mL   96 Tests Anmelden zum Anzeigen 10 bis 13 Tage
666,67 €
Details
Schwein 0.094 ng/mL 0.156-10 ng/mL   96 Tests Anmelden zum Anzeigen 10 bis 13 Tage
666,67 €
Details
Huhn 0.094 ng/mL 0.156-10 ng/mL   96 Tests Anmelden zum Anzeigen 10 bis 13 Tage
666,67 €
Details
Kaninchen 37.5 pg/mL 62.5-4000 pg/mL   96 Tests Anmelden zum Anzeigen 10 bis 13 Tage
666,67 €
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Affe 0.094 ng/mL 0.156-10 ng/mL   96 Tests Anmelden zum Anzeigen 10 bis 13 Tage
666,67 €
Details
Rind (Kuh)
  96 Tests Anmelden zum Anzeigen 13 bis 17 Tage
673,47 €
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Maus
  96 Tests Anmelden zum Anzeigen 13 bis 17 Tage
788,70 €
Details

Am meisten referenzierte Titin ELISA Kits

  1. Human Titin ELISA Kit für 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. in Proteome science 2012 (PubMed)

Weitere ELISA Kits für Titin Interaktionspartner

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. 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.

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

  3. 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.

  4. 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.

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

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

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

  8. 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.

  9. 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 ELISA Kits)+)-regulated, titin-based stiffness in skeletal muscle

Human Titin (TTN) Interaktionspartner

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

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

  3. 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.

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

  5. TTN truncating variants were observed in nearly one fourth of young dilated cardiomyopathy patient population, in vast majority without conduction system disease.

  6. detected an Linkage Disequilibrium block associated with a rapid functional decline in patients with sporadic ALS (zeige IGFALS ELISA Kits), which is linked to decreased expression of TTN.

  7. An estimated probability of pathogenicity of TTN truncating mutations affecting all transcripts of TTN, identified in unselected dilated cardiomyopathy patients is 97.8%.

  8. TTN variant segregated with hypertrophic cardiomyopathy in affected members of the family.

  9. A distinct phenotype for patients with distal myopathy is associated with novel recessive TTN variants including a Serbian founder variant.

  10. The results showed that MYBPC3 25-bp deletion polymorphism was significantly associated with elevated risk of left ventricular dysfunction (LVD), while TTN 18 bp I/D, TNNT2 5 bp I/D and myospryn K2906N polymorphisms did not show any significant association with LVD.

Pig (Porcine) Titin (TTN) Interaktionspartner

  1. Two polymorphisms previously identified and described in the 3'UTR (zeige UTS2R ELISA Kits) of MYPN (zeige MYPN ELISA Kits) 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.

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 ELISA Kits)+) 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 ELISA Kits) or CaMKIIdelta Lowers the Single Molecule and Cardiac Muscle Force

  5. Cleavage of C-terminal titin by CAPN3 (zeige CAPN3 ELISA Kits) 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 ELISA Kits) localizes to the M-band of the sarcomere through interaction with the M10 region of titin

Titin (TTN) Antigen-Profil

Beschreibung des Gens

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 (TTN) ELISA Kits

  • bent (bt) Antikörper
  • sallimus (sls) Antikörper
  • connectin (LOC530831) Antikörper
  • titin (titin) Antikörper
  • TITIN protein (TITIN) Antikörper
  • titin (TTN) Antikörper
  • titin (TTNLOC100620261) Antikörper
  • titin (Ttn) Antikörper
  • 0020/01 Antikörper
  • 39c-18 Antikörper
  • 1100001C23Rik Antikörper
  • 2310036G12Rik Antikörper
  • 2310057K23Rik Antikörper
  • 2310074I15Rik Antikörper
  • AF006999 Antikörper
  • anon-CREST Antikörper
  • AV006427 Antikörper
  • Bt Antikörper
  • CG1479 Antikörper
  • CG1915 Antikörper
  • CG10285 Antikörper
  • CG18242 Antikörper
  • CG18245 Antikörper
  • CG18857 Antikörper
  • CG32019 Antikörper
  • CMD1G Antikörper
  • CMH9 Antikörper
  • CMPD4 Antikörper
  • CT3598 Antikörper
  • CT8086 Antikörper
  • CT41299 Antikörper
  • d-titin Antikörper
  • D330041I19Rik Antikörper
  • D830007G01Rik Antikörper
  • Dmel\\CG1915 Antikörper
  • Dmel\\CG32019 Antikörper
  • EOMFC Antikörper
  • HMERF Antikörper
  • ket Antikörper
  • kettin Antikörper
  • KZ Antikörper
  • l(2)2 Antikörper
  • l(2)23 Antikörper
  • l(3)62Ca Antikörper
  • l(3)Ca Antikörper
  • l(3)dre8 Antikörper
  • l(3)j1D7 Antikörper
  • l(3)rL182 Antikörper
  • l(3)S002001 Antikörper
  • l(4)2 Antikörper
  • l(4)21 Antikörper
  • l(4)23 Antikörper
  • l(4)37 Antikörper
  • l(4)38 Antikörper
  • l(4)102CDa Antikörper
  • l(4)PT-2 Antikörper
  • L56 Antikörper
  • LGMD2J Antikörper
  • LOC530831 Antikörper
  • MCP Antikörper
  • mdm Antikörper
  • MYLK5 Antikörper
  • Prj Antikörper
  • sal Antikörper
  • sam Antikörper
  • shru Antikörper
  • Sls Antikörper
  • TITIN Antikörper
  • TMD Antikörper
  • UNC-22 Antikörper

Bezeichner auf Proteinebene für Titin (TTN) ELISA Kits

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 , connectin , TITIN protein , rhabdomyosarcoma antigen MU-RMS-40.14 , titin protein homolog

GENE ID SPEZIES
43814 Drosophila melanogaster
44013 Drosophila melanogaster
530831 Bos taurus
1791505 Rhodopirellula baltica SH 1
100101565 Oryctolagus cuniculus
424126 Gallus gallus
7273 Homo sapiens
100620261 Sus scrofa
100008570 Oryctolagus cuniculus
84015 Rattus norvegicus
22138 Mus musculus
540561 Bos taurus
100722767 Cavia porcellus
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