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TTN recombinant protein :: Titin Recombinant Protein

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Catalog # MBS1265279
Unit / Price
  0.01 mg  /  $175 +1 FREE 8GB USB
  0.05 mg  /  $225 +1 FREE 8GB USB
  0.1 mg  /  $360 +1 FREE 8GB USB
  0.2 mg  /  $575 +1 FREE 8GB USB
  0.5 mg  /  $945 +1 FREE 8GB USB
  1 mg  /  $1,445 +1 FREE 8GB USB
Product Name

Titin (TTN), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human Titin

Product Synonym Names
Connectin; Rhabdomyosarcoma antigen MU-RMS-40.14
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
MBS1265279 COA
Sequence Positions
5398-5604aa; Partial of Isoform 6
3D Structure
ModBase 3D Structure for Q8WZ42
E Coli
Greater than 90% as determined by SDS-PAGE. (lot specific)
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterile filter available upon request.
Low endotoxin available upon request.
Production Note
Special Offer: The E. coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E. coli host-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E. coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E. coli host-expressed protein for the fastest delivery among all hosts. Please contact us or email to support@mybiosource.com for more details.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of TTN recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
TTN recombinant protein
Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, ses to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
Product Categories/Family for TTN recombinant protein

TTN recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for TTN. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
NCBI Official Full Name
titin isoform N2BA
NCBI Official Synonym Full Names
NCBI Official Symbol
NCBI Official Synonym Symbols
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NCBI Protein Information
UniProt Protein Name
UniProt Synonym Protein Names
Connectin; Rhabdomyosarcoma antigen MU-RMS-40.14
Protein Family
UniProt Gene Name
UniProt Entry Name
NCBI Summary for TTN
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. [provided by RefSeq, Feb 2012]
UniProt Comments for TTN
Titin: a protein kinase that is abundant in striated muscle. 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. A 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. Mutations are associated with familial hypertrophic cardiomyopathy 9 and autoantibodies to titin are produced in patients with the autoimmune disease scleroderma.

Protein type: Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Protein kinase, CAMK; EC; CAMK group; MLCK family

Chromosomal Location of Human Ortholog: 2q31

Cellular Component: condensed nuclear chromosome; cytosol; extracellular region; I band; M band; muscle myosin complex; striated muscle thin filament; Z disc

Molecular Function: actin filament binding; actinin binding; ATP binding; calcium ion binding; calmodulin binding; enzyme binding; identical protein binding; muscle alpha-actinin binding; protease binding; protein binding; protein kinase binding; protein self-association; protein serine/threonine kinase activity; protein-tyrosine kinase activity; structural constituent of muscle; telethonin binding

Biological Process: blood coagulation; cardiac muscle contraction; cardiac muscle fiber development; cardiac muscle morphogensis; cardiac myofibril assembly; mitotic chromosome condensation; muscle contraction; muscle filament sliding; muscle thick filament assembly; muscle thin filament assembly; peptidyl-tyrosine phosphorylation; platelet activation; platelet degranulation; regulation of catalytic activity; regulation of protein kinase activity; response to calcium ion; sarcomere organization; sarcomerogenesis; striated muscle contraction

Disease: Cardiomyopathy, Dilated, 1g; Hereditary Myopathy With Early Respiratory Failure; Muscular Dystrophy, Limb-girdle, Type 2j; Myopathy, Early-onset, With Fatal Cardiomyopathy; Tibial Muscular Dystrophy, Tardive
Product References and Citations for TTN recombinant protein
Titins, giant proteins in charge of muscle ultrastructure and elasticity.Labeit S., Kolmerer B.Science 270:293-296(1995) Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity.Freiburg A., Trombitas K., Hell W., Cazorla O., Fougerousse F., Centner T., Kolmerer B., Witt C., Beckmann J.S., Gregorio C.C., Granzier H., Labeit S.Circ. Res. 86:1114-1121(2000) The complete gene sequence of titin, expression of an unusual ~700 kDa titin isoform and its interaction with obscurin identify a novel Z-line to I-band linking system.Bang M.-L., Centner T., Fornoff F., Geach A.J., Gotthardt M., McNabb M., Witt C.C., Labeit D., Gregorio C.C., Granzier H., Labeit S.Circ. Res. 89:1065-1072(2001) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers.Gautel M., Goulding D., Bullard B., Weber K., Furst D.O.J. Cell Sci. 109:2747-2754(1996) Dissecting titin into its structural motifs identification of an alpha helix near the N-terminus.Musco G., Tziatzos C., Schuck P., Pastore A.Biochemistry 34:553-561(1995) Familial dilated cardiomyopathy locus maps to chromosome 2q31.Siu B.L., Niimura H., Osborne J.A., Fatkin D., MacRae C., Solomon S., Benson D.W., Seidman J.G., Seidman C.E.Circulation 99:1022-1026(1999) Species variations in cDNA sequence and exon splicing patterns in the extensible I-band region of cardiac titin relation to passive tension.Greaser M.L., Berri M., Warren C.M., Mozdziak P.E.J. Muscle Res. Cell Motil. 23:473-482(2002) Lubec G., Chen W.-Q., Sun Y. Titin antibodies in myasthenia gravis identification of a major immunogenic region of titin.Gautel M., Lakey A., Barlow D.P., Holmes Z., Scales S., Leonard K., Labeit S., Mygland A., Gilhus N.E., Aarli J.A.Neurology 43:1581-1585(1993) Towards a molecular understanding of titin.Labeit S., Gautel M., Lakey A., Trinick J.EMBO J. 11:1711-1716(1992) Phosphorylation of KSF motifs in the C-terminal region of titin in differentiating myoblasts.Gautel M., Leonard K., Labeit S.EMBO J. 12:3827-3834(1993) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin.Mues A., van der Ven P.F.M., Young P., Furst D.O., Gautel M.FEBS Lett. 428:111-114(1998) Interaction of nebulin SH3 domain with titin PEVK and myopalladin implications for the signaling and assembly role of titin and nebulin.Ma K., Wang K.FEBS Lett. 532:273-278(2002) Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2.Lange S., Auerbach D., McLoughlin P., Perriard E., Schafer B.W., Perriard J.-C., Ehler E.J. Cell Sci. 115:4925-4936(2002) The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin.Kontrogianni-Konstantopoulos A., Bloch R.J.J. Biol. Chem. 278:3985-3991(2003) The muscle ankyrin repeat proteins CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules.Miller M.K., Bang M.-L., Witt C.C., Labeit D., Trombitas C., Watanabe K., Granzier H., McElhinny A.S., Gregorio C.C., Labeit S.J. Mol. Biol. 333:951-964(2003) Association of the chaperone alphaB-crystallin with titin in heart muscle.Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M., Labeit D., Ding L., Labeit S., Horwitz J., Leonard K.R., Linke W.A.J. Biol. Chem. 279:7917-7924(2004) MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly towards understanding MURF-dependent muscle ubiquitination.Witt S.H., Granzier H., Witt C.C., Labeit S.J. Mol. Biol. 350:713-722(2005) Nuclear titin interacts with A- and B-type lamins in vitro and in vivo.Zastrow M.S., Flaherty D.B., Benian G.M., Wilson K.L.J. Cell Sci. 119:239-249(2006) Mechanical stress-strain sensors embedded in cardiac cytoskeleton Z disk, titin, and associated structures.Hoshijima M.Am. J. Physiol. 290:H1313-H1325(2006) Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies.Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A., Hackman P., Ehler E., Richard I., Udd B.J. Biol. Chem. 285:30304-30315(2010) Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin a new member of the I set.Pfuhl M., Pastore A.Structure 3:391-401(1995) Structural basis for activation of the titin kinase domain during myofibrillogenesis.Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O., Wilmanns M., Gautel M.Nature 395:863-869(1998) The three-dimensional structure of a type I module from titin a prototype of intracellular fibronectin type III domains.Goll C.M., Pastore A., Nilges M.Structure 6:1291-1302(1998) Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.Mayans O., Wuerges J., Canela S., Gautel M., Wilmanns M.Structure 9:331-340(2001) Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk.Zou P., Pinotsis N., Lange S., Song Y.-H., Popov A., Mavridis I., Mayans O.M., Gautel M., Wilmanns M.Nature 439:229-233(2006) Structural analysis of the titin gene in hypertrophic cardiomyopathy identification of a novel disease gene.Satoh M., Takahashi M., Sakamoto T., Hiroe M., Marumo F., Kimura A.Biochem. Biophys. Res. Commun. 262:411-417(1999) Tibial muscular dystrophy is a titinopathy caused by mutations in TTN, the gene encoding the giant skeletal-muscle protein titin.Hackman P., Vihola A., Haravuori H., Marchand S., Sarparanta J., De Seze J., Labeit S., Witt C., Peltonen L., Richard I., Udd B.Am. J. Hum. Genet. 71:492-500(2002) Titin mutations as the molecular basis for dilated cardiomyopathy.Itoh-Satoh M., Hayashi T., Nishi H., Koga Y., Arimura T., Koyanagi T., Takahashi M., Hohda S., Ueda K., Nouchi T., Hiroe M., Marumo F., Imaizumi T., Yasunami M., Kimura A.Biochem. Biophys. Res. Commun. 291:385-393(2002) Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy.Gerull B., Gramlich M., Atherton J., McNabb M., Trombitas K., Sasse-Klaassen S., Seidman J.G., Seidman C., Granzier H., Labeit S., Frenneaux M., Thierfelder L.Nat. Genet. 30:201-204(2002) Tibial muscular dystrophy in a Belgian family.Van den Bergh P.Y.K., Bouquiaux O., Verellen C., Marchand S., Richard I., Hackman P., Udd B.Ann. Neurol. 54:248-251(2003) Functional analysis of titin/connectin N2-B mutations found in cardiomyopathy.Matsumoto Y., Hayashi T., Inagaki N., Takahashi M., Hiroi S., Nakamura T., Arimura T., Nakamura K., Ashizawa N., Yasunami M., Ohe T., Yano K., Kimura A.J. Muscle Res. Cell Motil. 26:367-374(2005) The kinase domain of titin controls muscle gene expression and protein turnover.Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E., Kristensen J., Brandmeier B., Franzen G., Hedberg B., Gunnarsson L.G., Hughes S.M., Marchand S., Sejersen T., Richard I., Edstroem L., Ehler E., Udd B., Gautel M.Science 308:1599-1603(2005) C-terminal titin deletions cause a novel early-onset myopathy with fatal cardiomyopathy.Carmignac V., Salih M.A.M., Quijano-Roy S., Marchand S., Al Rayess M.M., Mukhtar M.M., Urtizberea J.A., Labeit S., Guicheney P., Leturcq F., Gautel M., Fardeau M., Campbell K.P., Richard I., Estournet B., Ferreiro A.Ann. Neurol. 61:340-351(2007) Patterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) Diagnostic exome sequencing in persons with severe intellectual disability.de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.N. Engl. J. Med. 367:1921-1929(2012) +Additional computationally mapped references.<p>Provides general information on the entry.

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