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D5694

Sigma-Aldrich

Anti-DCP1A (N-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Anti-DCP1 Decapping enzyme 1, homolog A, Anti-SMAD 4-interacting transciption factor, Anti-SMAD 4-interacting transciptional co-activator, Anti-SMAD4IP1, Anti-SMIF

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

peso molecular

antigen ~70 kDa

reatividade de espécies

rat, human, mouse

concentração

~1.0 mg/mL

técnica(s)

immunoprecipitation (IP): 5-10 μg using lysates of HEK-293T
indirect immunofluorescence: 2-5 μg/mL using paraformaldehyde-fixed NIH-3T3 cells over-expressign human DCP1A
western blot: 1-2 μg/mL using lysates of HEK-293T cells over-expressing human DCP1A

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... DCP1A(55802)
mouse ... Dcp1a(75901)
rat ... Dcp1a(361109)

Descrição geral

Dcp1 colocalizes with Dcp2 in distinct cytoplasmic foci along with other proteins involved in the 5′ to 3′ mRNA decay. These foci are termed PB (processing bodies) or DCP-bodies. DCP1A and DCP1B are the two distinct genes of human DCP1. They share ~70% homology in their N-termini and ~30% homology in their full length.
Human cells consists of two decapping protein 1a (DCP1a) homologues, hDcp1a and hDcp1b, that are coded by two distinct genes.

Aplicação

Anti-DCP1A (N-terminal) antibody produced in rabbit has been used in:
  • immunoblotting
  • immunofluorescence
  • immunoprecipitation

Ações bioquímicas/fisiológicas

Dcp1 cleaves the m7G mRNA cap in the 5′ to 3′ mRNA decay pathway. Decapping is a critical and highly regulated step in the turnover of mRNA which involves decapping enzymes that hydrolyze the cap structure at the 5′ mRNA.
Human decapping protein 1a (hDCP1a) acts as a processing body (PB) marker.

forma física

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Exoneração de responsabilidade

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 classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Christy Fillman et al.
Current opinion in cell biology, 17(3), 326-331 (2005-05-20)
Decapping is a central step in eukaryotic mRNA turnover. Recent studies have identified several factors involved in catalysis and regulation of decapping. These include the following: an mRNA decapping complex containing the proteins Dcp1 and Dcp2; a nucleolar decapping enzyme
Adva Aizer et al.
PloS one, 8(1), e49783-e49783 (2013-01-10)
Processing bodies (PBs) are non-membranous cytoplasmic structures found in all eukaryotes. Many of their components such as the Dcp1 and Dcp2 proteins are highly conserved. Using live-cell imaging we found that PB structures disassembled as cells prepared for cell division
Jens Lykke-Andersen
Molecular and cellular biology, 22(23), 8114-8121 (2002-11-06)
Decapping is a key step in general and regulated mRNA decay. In Saccharomyces cerevisiae it constitutes a rate-limiting step in the nonsense-mediated decay pathway that rids cells of mRNAs containing premature termination codons. Here two human decapping enzymes are identified
Martin Fenger-Grøn et al.
Molecular cell, 20(6), 905-915 (2005-12-21)
Decapping is a key step in mRNA turnover. However, the composition and regulation of the human decapping complex is poorly understood. Here, we identify three proteins that exist in complex with the decapping enzyme subunits hDcp2 and hDcp1: hEdc3, Rck/p54

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