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Key Documents

T2780

Sigma-Aldrich

Monoclonal Anti-Tropomyosin antibody produced in mouse

clone TM311, ascites fluid

Synonyme(s) :

Anti-Tropomyosin Antibody

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

TM311, monoclonal

Poids mol.

antigen 36-39 kDa

Contient

15 mM sodium azide

Espèces réactives

pig, chicken, bovine, rabbit, mouse, hamster, rat, human

Technique(s)

immunoprecipitation (IP): suitable
indirect ELISA: suitable
indirect immunofluorescence: 1:400 using chicken fibroblasts
microarray: suitable
western blot: suitable using human tissue and chicken gizzard extracts

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

bovine ... TPM1(281544)
chicken ... TPM1(396366)
human ... TPM1(7168)
mouse ... Tpm1(22003)
rat ... Tpm1(24851)

Description générale

Monoclonal Anti-Tropomyosin (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Tropomyosin is a rigid rod-shaped protein closely associated with actin filaments. Non-muscle forms of tropomyosin have been identified in a wide range of cell types. Tropomyosin is made of two α helical polypeptide chains.

Immunogène

chicken gizzard tropomyosin.

Application

Monoclonal Anti-Tropomyosin has been used:
  • in immunofluorescent labelling
  • in immunohistochemistry
  • in western blotting
  • in immunoblotting

Mouse monoclonal clone TM311 anti-Tropomyosin antibody is used to tag tropomyosin for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques such as immunoblotting, immunoprecipitation, and immunofluorescence. It is used as a probe to determine the presence and roles of tropomyosin in cytoskeletal structures.

Actions biochimiques/physiologiques

Tropomyosin together with troponin, regulate the binding of myosin to actin. Tropomyosin is a dimeric coiled-coil protein forming continuous polymers along the myosin-binding groove of actin. Various tropomyosin isoforms help to confer structure and function to actins in the cytoskeleton and in striated muscle function.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Activation of MAP kinases and phosphorylation of caldesmon in canine colonic smooth muscle.
Gerthoffer W T, et al.
The Journal of Physiology, 495(3), 597-609 (1996)
Ewelina Jurewicz et al.
Biochimica et biophysica acta, 1833(3), 761-766 (2012-12-26)
The CacyBP/SIP protein interacts with several targets, including actin. Since the majority of actin filaments are associated with tropomyosin, in this work we characterized binding of CacyBP/SIP to the actin-tropomyosin complex and examined the effects of CacyBP/SIP on actin filament
Tropomyosin-master regulator of actin filament function in the cytoskeleton
Gunning P W, et al.
Journal of Cell Science, 128(16), 2965-2974 (2015)
CENP-A is essential for cardiac progenitor cell proliferation
McGregor M, et al
Cell Cycle, 13(5), 739-748 (2014)
Non-canonical Wnt signaling enhances differentiation of Sca1+/c-kit+ adipose-derived murine stromal vascular cells into spontaneously beating cardiac myocytes
Palpant N J, et al.
Journal of Molecular and Cellular Cardiology, 43(3), 362-370 (2007)

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