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Titin Proteins (TTN)

TTN encodes a large abundant protein of striated muscle. Additionally we are shipping Titin Antibodies (59) and Titin Kits (15) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
TTN 7273 Q8WZ42
Rat TTN TTN 84015  
Mouse TTN TTN 22138  
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Top Titin Proteins at

Showing 4 out of 7 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag 50 μg Log in to see 21 to 26 Days
HOST_Escherichia coli (E. coli) Human His tag 100 μg Log in to see 11 to 13 Days
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
HOST_Escherichia coli (E. coli) Human Un-conjugated   100 μg Log in to see 9 to 16 Days

TTN Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,

More Proteins for Titin (TTN) Interaction Partners

Fruit Fly (Drosophila melanogaster) Titin (TTN) interaction partners

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

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

  3. 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.

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

  5. 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) interaction partners

  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) interaction partners

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

  2. 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.

  3. 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.

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

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

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

  7. 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.

  8. 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 (show CA2 Proteins)+)-regulated, titin-based stiffness in skeletal muscle

Human Titin (TTN) interaction partners

  1. Results show that the titin I27Y9P variant has similar mechanical stability as the wildtype.

  2. Phosphorylating Titin's Cardiac N2B Element by ERK2 (show MAPK1 Proteins) or CaMKIIdelta Lowers the Single Molecule and Cardiac Muscle Force

  3. Suggest a potential biological role for some TTN missense variants in dilated cardiomyopathy.

  4. Data suggest that titin functions as an integrated protein chain where functionalities emerge from the joint action of titan and other sarcomere/A-band components (such as TCAP (show TCAP Proteins)); titin exhibits tertiary elasticity and molecular shape memory. [REVIEW]

  5. a large number of VUS in the TTN gene were identified from a cohort of samples from patients suffering cardiac diseases associated with sudden cardiac death.

  6. TTN mutations have been strongly associated with four cardiomyopathies: Dilated cardiomyopathy, Hypertrophic cardiomyopathy, Arrhythmogenic right ventricular cardiomyopathy and Restrictive cardiomyopathy.

  7. Cleavage of C-terminal titin by CAPN3 (show CAPN3 Proteins) is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy.

  8. findings indicate that titin mutations cause dilated cardiomyopathy by disrupting critical linkages between sarcomerogenesis and adaptive remodeling

  9. Engineered all four of the naturally occurring human M10 (the extreme C-terminus of titin) missense mutants and biophysically characterized them in vitro.

  10. an increase in intracellular Ca(2 (show CA2 Proteins)+) concentration leads to Ca(2 (show CA2 Proteins)+) binding to the PEVK region of titin.

Pig (Porcine) Titin (TTN) interaction partners

  1. Two polymorphisms previously identified and described in the 3'UTR of MYPN (show MYPN Proteins) 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) interaction partners

  1. Phosphorylating Titin's Cardiac N2B Element by ERK2 (show MAPK1 Proteins) or CaMKIIdelta Lowers the Single Molecule and Cardiac Muscle Force

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

  3. titin affects the tuning of shivering frequency

  4. 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.

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

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

  7. alpha-Synemin (show SYNM Proteins) localizes to the M-band of the sarcomere through interaction with the M10 region of titin

  8. Data reveal that Titin protein is a pseudokinase with non-detectable catalytic output but is a high-affinity binding locus for MuRF1 (show TRIM63 Proteins).

  9. [review] A mouse model lacking nine titin immunoglobulin domains (IG KO) shows the effects of a small increase in titin stiffness; the mutant mice show changes in muscle contractivity.

  10. Resting and dynamic LV torsional mechanics is impaired in patients with beta-thalassaemia major. Cell and animal models suggest a potential role of titin degradation in iron overload-induced alteration of LV torsional mechanics.

Titin (TTN) Protein Profile

Protein Summary

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.

Gene names and symbols associated with Titin Proteins (TTN)

  • bent (bt)
  • sallimus (sls)
  • connectin (LOC530831)
  • titin (titin)
  • TITIN protein (TITIN)
  • titin (TTN)
  • titin (TTNLOC100620261)
  • titin (Ttn)
  • 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
  • LOC530831 protein
  • MCP protein
  • mdm protein
  • MYLK5 protein
  • Prj protein
  • sal protein
  • sam protein
  • shru protein
  • Sls protein
  • TITIN protein
  • TMD protein
  • UNC-22 protein

Protein level used designations for Titin Proteins (TTN)

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

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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