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Merck

D5694

Sigma-Aldrich

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

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

Synonym(e):

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

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~70 kDa

Speziesreaktivität

rat, human, mouse

Konzentration

~1.0 mg/mL

Methode(n)

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-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

12 - Non Combustible Liquids

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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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