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DENR Antibody

     
  • 1 - DENR Antibody ASC11786
    Western blot analysis of DENR in human brain tissue lysate with DENR antibody at 1 µg/ml.
  • 2 - DENR Antibody ASC11786
    Immunohistochemistry of DENR in rat brain tissue with DENR antibody at 5 µg/mL.
  • 3 - DENR Antibody ASC11786
    Immunofluorescence of DENR in rat brain tissue with DENR antibody at 20 µg/mL.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IF, E, IHC-P
Primary Accession O43583
Other Accession NP_003668, 27501446
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Isotype IgG
Calculated MW 22092 Da
Concentration (mg/ml) 1 mg/mL
Conjugate Unconjugated
Application Notes DENR antibody can be used for detection of DENR by Western blot at 1 - 2 µg/ml. Antibody can also be used for Immunohistochemistry at 5 µg/mL. For Immunoflorescence start at 20 µg/mL.
Additional Information
Gene ID 8562
Other Names Density-regulated protein, DRP, Protein DRP1, Smooth muscle cell-associated protein 3, SMAP-3, DENR, DRP1
Target/Specificity DENR; DENR antibody is human, mouse and rat reactive.
Reconstitution & Storage DENR antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.
PrecautionsDENR Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name DENR
Synonyms DRP1
Function Translation regulator forming a complex with MCTS1 to promote translation reinitiation. Translation reinitiation is the process where the small ribosomal subunit remains attached to the mRNA following termination of translation of a regulatory upstream ORF (uORF), and resume scanning on the same mRNA molecule to initiate translation of a downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is pivotal to two linked mechanisms essential for translation reinitiation. Firstly, the dissociation of deacylated tRNAs from post- termination 40S ribosomal complexes during ribosome recycling. Secondly, the recruitment in an EIF2-independent manner of aminoacylated initiator tRNA to P site of 40S ribosomes for a new round of translation. This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent.
Cellular Location Cytoplasm.
Tissue Location Highly expressed in heart and skeletal muscle and moderately expressed in the brain, placenta, liver and pancreas. Weakly expressed in the lung and kidney.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

DENR (density-regulated protein), also designated DRP or smooth muscle cell associated protein 3 (SMAP-3), is a 198 amino acid protein that may be involved in the translation of target mRNAs by scanning and recognition of the initiation codon (1). It plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1 (2,3). DENR contains a SUI1 domain and is found in a variety of tissues with highest levels present in skeletal and cardiac muscle. It is up-regulated in ovarian and breast cancer cells by ERBB2 overexpression (4).

REFERENCES

Deyo JE, Chiao PJ, Tainsky MA. DRP, a novel protein expressed at high cell density but not during growth arrest. DNA Cell Biol. 1998; 17:437-47.
Skabkin MA, Skabkina OV, Dhote V, et al. Activities of Ligatin and MCT-1/DENR in eukaryotic translation initiation and ribosomal recycling. Genes Dev. 2010; 24:1787-801.
Mazan-Mamczarz K and Gartenhaus RB. Post-transcriptional control of the MCT1-associated protein DENR/DRP by RNA-binding protein AUF1. Cancer Genomics Proteomics 2007; 4:233-9.
Oh JJ, Grosshans DR, Wong SG et al. Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells. Nucleic Acids Res. 1999; 27:4008-17.

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