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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

Synonyma:

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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~70 kDa

species reactivity

rat, human, mouse

concentration

~1.0 mg/mL

technique(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

UniProt accession no.

Q9NPI6

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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Navštívit knihovnu dokumentů

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
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
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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