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Key Documents

T9283

Sigma-Aldrich

Monoclonal Anti-Tropomyosin (Sarcomeric) antibody produced in mouse

clone CH1, ascites fluid

Synonym(s):

Anti-C15orf13, Anti-CMD1Y, Anti-CMH3, Anti-HEL-S-265, Anti-HTM-alpha, Anti-LVNC9, Anti-TMSA

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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

CH1, monoclonal

contains

15 mM sodium azide

species reactivity

human, chicken, rat

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50 using sections of human tongue
immunohistochemistry (frozen sections): suitable using human and animal tissue sections
immunoprecipitation (IP): suitable
microarray: suitable
western blot: suitable using native preparations

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

chicken ... TPM1(396366)
human ... TPM1(7168)
rat ... Tpm1(24851)

General description

Tropomyosin 1 (TPM1) is encoded by the gene mapped to human chromosome 15q22.2. The encoded protein belongs to the TPM protein family.

Specificity

The antibody recognizes an epitope on skeletal and cardiac tropomyosin. The antibody shows no reaction with denatured protein by immunoblotting. No cross-reactivity has been observed with smooth muscle or non-muscle tropomyosin.

Immunogen

chicken muscle tropomyosin.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Monoclonal Anti-Tropomyosin (sarcomeric) antibody produced in mouse has been used in immunofluorescence and immunohistochemistry.

Biochem/physiol Actions

Tropomyosin 1 (TPM1) is a potent tumor suppressor gene. It is expressed at low levels in various types of solid cancers including, oral squamous cell carcinoma (OSCC) and tongue squamous cell carcinoma. Mutation in the gene is associated with the development of hypertrophic cardiomyopathy. The encoded protein is involved in the regulation of actin-myosin interaction in striated muscles. Tropomyosin plays an essential role in Ca2+ -regulated contraction of cardiac muscle.

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

12 - Non 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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Tropomyosin-1 acts as a potential tumor suppressor in human oral squamous cell carcinoma
Pan H
PLoS ONE, 12, e0168900-e0168900 (2017)
Myofibril Degeneration Caused by Tropomodulin Overexpression Leads to Dilated Cardiomyopathy in Juvenile Mice
Sussman MA
The Journal of Clinical Investigation, 101, 51-61 (1998)
Natalie Gude et al.
Circulation research, 99(4), 381-388 (2006-07-15)
Activation of Akt is associated with enhanced cell cycling and cellular proliferation in nonmyocytes, but this effect of nuclear Akt accumulation has not been explored in the context of the myocardium. Cardiac-specific expression of nuclear-targeted Akt (Akt/nuc) in transgenics prolongs
Nilgün Gedik et al.
Scientific reports, 7(1), 7629-7629 (2017-08-11)
Remote ischemic preconditioning (RIPC) by repeated brief cycles of limb ischemia/reperfusion reduces myocardial ischemia/reperfusion injury. In left ventricular (LV) biopsies from patients undergoing coronary artery bypass grafting (CABG), only the activation of signal transducer and activator of transcription 5 was
Structural and Functional Effects of Cardiomyopathy-Causing Mutations in the Troponin T-Binding Region of Cardiac Tropomyosin.
Matyushenko AM
Biochemistry, 56, 250-259 (2017)

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