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Merck

T9030

Anti-Titin antibody, Mouse monoclonal

clone T11, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-Titin antibody produced in mouse, 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

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
MFCD00164750
Conjugate:
unconjugated
Clone:
T11, monoclonal
Application:
EM, IF, IHC (f), WB
Citations:
22

Key Documents

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biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

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

Quality Level

200

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.

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.
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.
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).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000467695
0000467695
0000442801
0000442801
0000216736

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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)
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)
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)
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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