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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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0.2 ML
492.00 CHF

492.00 CHF


Date d'expédition estimée le17 avril 2025


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Changer de vue
0.2 ML
492.00 CHF

About This Item

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

492.00 CHF


Date d'expédition estimée le17 avril 2025


Devis pour commande en gros

Source biologique

mouse

Niveau de qualité

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)

Catégories apparentées

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[1]
  • 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


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Consulter la Bibliothèque de documents

A cardiac myosin binding protein C mutation in the Maine Coon cat with familial hypertrophic cardiomyopathy
Meurs KM, et al.
Human Molecular Genetics, 14, 3587-3593 (2005)
Titin Mutations as the Molecular Basis for Dilated Cardiomyopathy
Itoh-Satoh M
Biochemical and Biophysical Research Communications, 291, 385-393 (2002)
Smooth muscle titin forms in vitro amyloid aggregates
Bobylev AG
Bioscience Reports, 36 (2016)
Genome-wide linkage scan for maximum and length-dependent knee muscle strength in young men: significant evidence for linkage at chromosome 14q24.3
De Mars G
Journal of medical Genetics, 45, 275-283 (2008)
Folding-unfolding transitions in single titin molecules characterized with laser tweezers.
Kellermayer MS
Science, 276, 1112-1116 (1997)

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