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T9030

Sigma-Aldrich

Monoclonal Anti-Titin antibody produced in mouse

clone T11, ascites fluid

Synonym(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

MDL number:
MFCD00164750
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

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)

Related Categories

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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WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Titin Mutations as the Molecular Basis for Dilated Cardiomyopathy
Itoh-Satoh M
Biochemical and Biophysical Research Communications, 291, 385-393 (2002)
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)
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)
Folding-unfolding transitions in single titin molecules characterized with laser tweezers.
Kellermayer MS
Science, 276, 1112-1116 (1997)
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)
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