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T9030

Sigma-Aldrich

Monoclonal Anti-Titin antibody produced in mouse

clone T11, ascites fluid

Synonyme(s) :

Anti-CMD1G, Anti-CMH9, Anti-CMPD4, Anti-EOMFC, Anti-HMERF, Anti-LGMD2J, Anti-LGMDR10, Anti-MYLK5, Anti-SALMY, Anti-TMD

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About This Item

Numéro MDL:
MFCD00164750
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

T11, monoclonal

Contient

15 mM sodium azide

Espèces réactives

vertebrates, chicken

Technique(s)

electron microscopy: suitable
immunohistochemistry (frozen sections): suitable
indirect immunofluorescence: 1:1,000 using frozen tissue sections of animal skeletal muscle
western blot: suitable

Isotype

IgG2b

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

chicken ... TTN(424126)

Description générale

Monoclonal Anti-Titin (mouse IgG2b isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. It is a flexible, filamentous constituent of striated muscle that is thought to give rise to an elastic filament component underlying the myofibrillar organization.
Titin (TTN), also known as connectin, is encoded by the gene mapped to human chromosome 2q31.2. TTN is a giant elastic protein expressed in striated and smooth muscles of vertebrates. The encoded protein contains up to 300 immunoglobulin-like and fibronectin type-3-like (FN3) domains.

Spécificité

The antibody localizes titin (connectin) in skeletal and heart muscle of a wide variety of species from cold-blooded vertebrates to human. The antibody does not cross-react with nebulin. Likewise, it does not react with smooth muscle, non-muscle tissues, or cultured cells.

Immunogène

titin/nebulin fraction from chicken breast muscle.

Application

Monoclonal Anti-Titin antibody produced in mouse has been used in following studies.
  • western blotting
  • antibody staining
  • immunofluorescence microscopy
  • immunohistochemistry

Actions biochimiques/physiologiques

Monoclonal Anti-Titin can be used for study of the elastic filaments within sarcomeric structures. It is also useful as a differentiation marker in the separation of rhabdomyosarcomas from other muscle tumors.
Titin (TTN) helps in maintaining sarcomeric structural integrity by interacting with many other myofibrillar and cytoskeletal proteins. Additionally, it is also involved in developing the passive elastic force in muscle. Genetic variations in the gene has been associated with the development of dilated cardiomyopathy (DCM).

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Jun Zou et al.
eLife, 4, e09406-e09406 (2015-10-17)
Truncating mutations in the giant sarcomeric protein Titin result in dilated cardiomyopathy and skeletal myopathy. The most severely affected dilated cardiomyopathy patients harbor Titin truncations in the C-terminal two-thirds of the protein, suggesting that mutation position might influence disease mechanism.
Some distinctive features of zebrafish myogenesis based on unexpected distributions of the muscle cytoskeletal proteins actin, myosin, desmin, ?-actinin, troponin and titin
Costa ML
Mechanisms of Development, 116, 95-104 (2002)
Y Ishigai et al.
The American journal of physiology, 273(6 Pt 2), H2659-H2663 (1998-01-22)
To examine whether the bradykinin-nitric oxide (NO) pathway directly participates in the antihypertrophic property of angiotensin-converting enzyme (ACE) inhibitors in congestive heart failure, the effects of bradykinin were studied in rat cultured heart cells. Bradykinin (0.1, 1 nM) prevented the
Gigantic variety: expression patterns of titin isoforms in striated muscles and consequences for myofibrillar passive stiffness
Neagoe C
Journal of Muscle Research and Cell Motility, 24, 175-189 (2003)
Elastic domains of giant proteins in striated muscle: Modeling compliance with rulers
Chase PB
The Journal of General Physiology, 151(5), 619-622 (2019)
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