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Key Documents

SAB4200114

Sigma-Aldrich

Anti-EDC4 (N-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-Ge-1, Anti-HEDLS (Human enhancer of decapping, (large subunit), Anti-RCD-8

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~150 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 5-10 μg using ysates of HEK-293 cells over expressing human EDC4
indirect immunofluorescence: 2-5 μg/mL using paraformaldehyde fixed NIH-3T3 cells over expressing human EDC4
western blot: 0.5-1 μg/mL using lysates of HEK-293 cells over expressing human EDC4

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... EDC4(23644)
mouse ... Edc4(234699)
rat ... Edc4(361399)

General description

Enhancer of mRNA-decapping protein 4 (EDC4), also known as human enhancer of decapping large subunit (HEDLS) or Ge-1, is characterized with an N-terminal WD40 repeat and a C-terminal domain which interacts with mRNA-decapping enzyme subunit 2 (Dcp2), and mediates EDC4 oligomerization and P-body localization .
The EDC4 gene maps on human chromosome 16q22.1.

Specificity

Anti-EDC4 (N-terminal) specifically recognizes human EDC4.

Application

Anti-EDC4 (N-terminal) antibody has been used in:
  • immunoprecipitation
  • immunofluorescence
  • immunoblotting.

Biochem/physiol Actions

Human enhancer of mRNA-decapping protein 4 (EDC4) associates with hDcp2 and stimulates hDcp2 activity in vitro as well as mediating the interaction between mRNA-decapping enzyme subunit 1 & 2 (DCP1 and DCP2).
Interaction of processing-body components, EDC4 and Dcp1a is essential for the post-transcriptional regulation of interleukin (IL)-6.

Physical form

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

Storage and Stability

Store at –20 °C. For continuous use, the product may be stored at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing is not recommended. Storage in “frost-free” freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

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 Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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’.

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A human microprotein that interacts with the mRNA decapping complex
D'Lima N G, et al.
Nature Chemical Biology, 13(2), 174-174 (2017)
Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencing
Eulalio A, et al.
Genes & Development, 21(20), 2558-2570 (2007)
Jucimara Colombo et al.
Oncology reports, 21(3), 649-663 (2009-02-13)
Laryngeal squamous cell carcinoma is very common in head and neck cancer, with high mortality rates and poor prognosis. In this study, we compared expression profiles of clinical samples from 13 larynx tumors and 10 non-neoplastic larynx tissues using a
Nadia G D'Lima et al.
Nature chemical biology, 13(2), 174-180 (2016-12-06)
Proteomic detection of non-annotated microproteins indicates the translation of hundreds of small open reading frames (smORFs) in human cells, but whether these microproteins are functional or not is unknown. Here, we report the discovery and characterization of a 7-kDa human
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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