T6277
Monoclonal Anti-Troponin T antibody produced in mouse
clone JLT-12, ascites fluid
Sinónimos:
Anti-ANM, Anti-NEM5, Anti-STNT, Anti-TNT, Anti-TNTS
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About This Item
Productos recomendados
biological source
mouse
Quality Level
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
rat ... Tnnt1(171409) , Tnnt2(24837) , Tnnt3(24838)
Categorías relacionadas
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
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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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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