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Merck

T2780

Sigma-Aldrich

Monoclonal Anti-Tropomyosin antibody produced in mouse

clone TM311, ascites fluid

Sinónimos:

Anti-Tropomyosin Antibody

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

mouse

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

ascites fluid

tipo de anticuerpo

primary antibodies

clon

TM311, monoclonal

mol peso

antigen 36-39 kDa

contiene

15 mM sodium azide

reactividad de especies

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

técnicas

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

isotipo

IgG1

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

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

Categorías relacionadas

Descripción general

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.

Inmunógeno

chicken gizzard tropomyosin.

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

nwg

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

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Visite la Librería de documentos

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)
Vertebrate tropomyosin: distribution, properties and function
Perry, S Victor
Journal of Muscle Research and Cell Motility, 22(1), 5-49 (2001)
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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