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Merck

T9030

Sigma-Aldrich

Monoclonal Anti-Titin antibody produced in mouse

clone T11, ascites fluid

Sinónimos:

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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

T11, monoclonal

contains

15 mM sodium azide

species reactivity

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

chicken ... TTN(424126)

General description

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.

Specificity

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.

Immunogen

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

Biochem/physiol Actions

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).

Disclaimer

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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Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Elastic domains of giant proteins in striated muscle: Modeling compliance with rulers
Chase PB
The Journal of General Physiology, 151(5), 619-622 (2019)
Stephan Lange et al.
JCI insight, 4(19) (2019-09-13)
Perturbations in biomechanical stimuli during cardiac development contribute to congenital cardiac defects such as hypoplastic left heart syndrome (HLHS). This study sought to identify stretch-responsive pathways involved in cardiac development. miRNA-Seq identified miR-486 as being increased in cardiomyocytes exposed to
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)
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)
Titin Mutations as the Molecular Basis for Dilated Cardiomyopathy
Itoh-Satoh M
Biochemical and Biophysical Research Communications, 291, 385-393 (2002)

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