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>   首页   >   产品   >   一抗   >   精选抗体   >   MORF4L2 Antibody (C-term)   

MORF4L2 Antibody (C-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - MORF4L2 Antibody (C-term) AP14737b
    MORF4L2 Antibody (C-term) (Cat. #AP14737b) western blot analysis in 293 cell line lysates (35ug/lane).This demonstrates the MORF4L2 antibody detected the MORF4L2 protein (arrow).
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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, E
Primary Accession Q15014
Other Accession Q4R578, NP_001135901.1, NP_001135891.1, NP_001135898.1
Reactivity Rat, Human
Predicted Monkey
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 32308 Da
Antigen Region 259-288 aa
Additional Information
Gene ID 9643
Other Names Mortality factor 4-like protein 2, MORF-related gene X protein, Protein MSL3-2, Transcription factor-like protein MRGX, MORF4L2, KIAA0026, MRGX
Target/Specificity This MORF4L2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 259-288 amino acids from the C-terminal region of human MORF4L2.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsMORF4L2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name MORF4L2
Synonyms KIAA0026, MRGX
Function Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also a component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones.
Cellular Location Nucleus.
Research Areas

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

BACKGROUND

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome -DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones.

REFERENCES

Pezo, R.C., et al. Cancer Res. 68(13):4977-4982(2008)
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
Oh, J.H., et al. Mamm. Genome 16(12):942-954(2005)
Cai, Y., et al. J. Biol. Chem. 280(14):13665-13670(2005)
Tominaga, K., et al. J. Biol. Chem. 278(49):49618-49624(2003)

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