Skip to Content
Merck
All Photos(4)

Key Documents

D6319

Sigma-Aldrich

Anti-DCP2 (C-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-DCP2 decapping enzyme homolog (S. cerevisiae), Anti-NUDT20, Anti-Nucleleoside diphosphate-linked moiety X motif 20, Anti-Nudix motif 20

Sign Into View Organizational & Contract Pricing


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 ~50 kDa

species reactivity

rat, mouse, human

concentration

~1 mg/mL

technique(s)

indirect immunofluorescence: 2-5 μg/mL using paraformaldehyde-fixed NIH-3T3 celle
indirect immunofluorescence: suitable
western blot: 2-4 μg/mL using lysaes of K-562 and Rat1 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DCP2(167227)
mouse ... Dcp2(20640)
rat ... Dcp2(291604)

Related Categories

General description

Dcp2 colocalizes with Dcp1 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. hDCP2 contains a highly conserved Nudix (nucleoside diphosphate linked to an X moiety) motif critical for the decapping activity.

Immunogen

synthetic peptide corresponding to amino acids 406-420 of human DCP2, conjugated to KLH. The corresponding sequence is identical in rat and mouse.

Application

Anti-DCP2 (C-terminal) antibody has been used in immunocytochemistry and image correlation analysis. It may also be used in immunoblotting.
Anti-DCP2 antibody produced in rabbit is suitable for indirect immunofluorescence at a working concentration of 2-5μg/mL using paraformaldehyde-fixed NIH-3T3 cells over-expressing human DCP2 and western blot analysis at a working concentration of 2-4μg/mL using lysates of K-562 and Rat1 cells. Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.

Biochem/physiol Actions

Dcp2 is an RNA binding protein and can cleave only a cap structure that is linked to an RNA moiety, suggesting that Dcp2 can differentially associate with specific mRNAs. Dcp2 cleaves the m7G mRNA cap in the 5′ to 3′ mRNA decay pathway, in association with Dcp1 and Hedls complex. 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. Dcp2 is the catalytic subunit, and the mRNA is degraded by the major cytoplasmic 5′ to 3′ exonuclease XRN1. The enzymatic activity of DCP2 is critically dependent on the DCP1 subunit in vivo.

Target description

DCP2 (C-terminal) is a key component of an mRNA-decapping complex required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Ohannes K Melemedjian et al.
Neuroscience letters, 563, 169-174 (2013-10-02)
Processing (P) bodies are RNA granules that comprise key cellular sites for the metabolism of mRNAs. In certain cells, including neurons, these RNA granules may also play an important role in storage of mRNAs in a translationally dormant state. Utilizing
Lee Davidson et al.
The EMBO journal, 31(11), 2566-2578 (2012-04-24)
Eukaryotic protein-coding genes are transcribed as pre-mRNAs that are matured by capping, splicing and cleavage and polyadenylation. Although human pre-mRNAs can be long and complex, containing multiple introns and many alternative processing sites, they are usually processed co-transcriptionally. Mistakes during
You Li et al.
Molecular and cellular biology, 28(3), 939-948 (2007-11-28)
mRNA decapping is a critical step in the control of mRNA stability and gene expression and is carried out by the Dcp2 decapping enzyme. Dcp2 is an RNA binding protein that must bind RNA in order to recognize the cap
T Dunckley et al.
The EMBO journal, 18(19), 5411-5422 (1999-10-03)
The major pathway of mRNA degradation in yeast occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. To identify proteins that control the activity of the decapping enzyme, which is encoded by the DCP1
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service