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Merck
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C1862

Sigma-Aldrich

Anti-Coilin antibody, Mouse monoclonal

~1.5 mg/mL, clone pδ, purified from hybridoma cell culture

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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

purified from hybridoma cell culture

tipo de anticuerpo

primary antibodies

clon

pδ, monoclonal

formulario

buffered aqueous solution

mol peso

antigen ~80 kDa by SDS-PAGE

reactividad de especies

human

concentración

~1.5 mg/mL

técnicas

immunocytochemistry: suitable
microarray: suitable
western blot: 1-2 μg/mL using HeLa nuclear extract

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

human ... COIL(8161)

Descripción general

Monoclonal Anti-Coilin (mouse IgG1 isotype) is derived from the pδ hybridoma produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with coilin. Coilin contains two nuclear localization sequences (NLS) (at amino acid 107-112 and 181-198) and several serine residues that are phosphorylated in vivo. The description of specific intranuclear structures known today as Cajal bodies was first published in 1903 by the neuro-cytologist Ramon-γ-Cajal who discovered that neurons contained spherical structures of around 0.5 μm in diameter that were often associated with nucleoli, nucleolar accessory bodies. It was found that patients with auto-antibodies against coiled bodies recognize a protein of 80 kDa termed p80-coilin. Nuclear antigens shown to colocalize with p80 coilin in Cajal bodies include basal transcription factors, cell cycle factors (cdks), splicing snRNPs and nucleolar factors including snoRNP.

Especificidad

The antibody recognizes the C-terminal region of human coilin and does not recognize mouse coilin.

Inmunógeno

C-terminal (389 amino acids) human coilin

Aplicación

Monoclonal Anti-Coilin antibody produced in mouse has been used in:
  • immunoblotting
  • immunocytochemistry
  • cell microinjection
  • fluorescence imaging
  • indirect immunofluorescence

Acciones bioquímicas o fisiológicas

Mutating Serine-202 to Aspartate causes the disappearance of coiled bodies and a redistribution of coilin to intranucleolar domains. Coilin plays a key role in ribonucleoprotein and Cajal body formation.

Forma física

Supplied as a solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

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

12 - Non 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)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Cajal bodies and coilin?moving towards function
Ogg SC and Lamond AI
The Journal of cell biology, 159(1), 17-21 (2002)
F Almeida et al.
The Journal of cell biology, 142(4), 899-912 (1998-08-29)
The coiled body is a distinct subnuclear domain enriched in small nuclear ribonucleoprotein particles (snRNPs) involved in processing of pre-mRNA. Although the function of the coiled body is still unknown, current models propose that it may have a role in
P68 RNA helicase (DDX5) alters activity of cis-and trans-acting factors of the alternative splicing of H-Ras
Camats M, et al.
Testing, 3(8), e2926-e2926 (2008)
Coilin: The first 25 years
Machyna M, et al.
RNA Biology, 12(6), 590-596 (2015)
Gall, J.G.
Annual Review of Cell Biology, 16, 273-273 (2000)

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