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Key Documents

T6277

Sigma-Aldrich

Monoclonal Anti-Troponin T antibody produced in mouse

clone JLT-12, ascites fluid

Synonym(s):

Anti-ANM, Anti-NEM5, Anti-STNT, Anti-TNT, Anti-TNTS

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About This Item

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

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

JLT-12, monoclonal

contains

15 mM sodium azide

species reactivity

chicken, rat, bovine, rabbit

technique(s)

immunohistochemistry: suitable
western blot: 1:200 using rabbit total skeletal muscle extract

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Monoclonal Anti-Troponin T (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.
Troponin T is a vital subunit of troponin. Troponin T is a comma or rod shaped protein with a length of 185-205 Å. Troponin T is positioned in the actin helix groove and is extended along the filament of troponin. Life span of serum troponin T is 120 minutes. N- terminal end of the protein is enriched in negatively charged residues and C- terminal end is enriched with positively charged residues. This uneven distribution of charges in troponin T facilitates its aggregation at physiological salt concentration. In humans, cardiac troponin T exists in four isoforms, out of which three are expressed in the fetus and one isoform is expressed in the adult heart.

Immunogen

Troponin T from rabbit skeletal muscle.

Application

Monoclonal Anti-Troponin T antibody produced in mouse has been used in following studies:
  • Western blot analysis.
  • Immunocytochemical analysis.
  • Immunofluorescence.
Monoclonal Anti-Troponin T antibody produced in mouse has been used in immunostaining.

Biochem/physiol Actions

Troponin T is a subunit of troponin, which facilitates binding of troponin to tropomyosin. It also plays a crucial role in muscle contraction. Cardiac troponin T acts as a potential marker for the detection of acute myocardial infarction (MI). Apart from facilitating binding of troponin components to the actin-tropomyosin filament, it is has an essential role in the regulation of actomyosin ATPase activity. Cardiac troponin T gene mutation leads to hypertrophic cardiomyopathy.

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 Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Michael T Massengill et al.
Cardiovascular research, 111(1), 34-43 (2016-03-31)
Under pressure overload, initial adaptive hypertrophy of the heart is followed by cardiomyocyte elongation, reduced contractile force, and failure. The mechanisms governing the transition to failure are not fully understood. Pressure overload reduced cardiac myosin light chain kinase (cMLCK) by
J C Moolman et al.
Journal of the American College of Cardiology, 29(3), 549-555 (1997-03-01)
This study was designed to verify initial observations of the clinical and prognostic features of hypertrophic cardiomyopathy caused by cardiac tropnin T gene mutations. The most common cause of sudden cardiac death in the young is hypertrophic cardiomyopathy, which is
Lori A Walker et al.
American journal of physiology. Heart and circulatory physiology, 301(3), H832-H840 (2011-05-31)
Right ventricular (RV) failure is one of the strongest predictors of mortality both in the presence of left ventricular decompensation and in the context of pulmonary vascular disease. Despite this, there is a limited understanding of the biochemical and mechanical
Dynamics of the skeletal muscle secretome during myoblast differentiation
Henningsen J, et al.
Molecular and Cellular Proteomics, 9(11), 2482-2496 (2010)
V L Filatov et al.
Biochemistry. Biokhimiia, 64(9), 969-985 (1999-10-16)
This review discusses the structure and properties of the isolated components of troponin, their interaction, and the mechanisms of regulation of contractile activity of skeletal and cardiac muscle. Data on the structure of troponin C in crystals and in solution

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