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TRIP12 Antibody

Rabbit Polyclonal Antibody

     
  • IHC - TRIP12 Antibody ALS15172
    Anti-TRIP12 antibody IHC of human prostate.
  • SPECIFICATION
  • CITATIONS
  • PROTOCOLS
  • BACKGROUND
Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
IHC-P
Primary Accession Q14669
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 220kDa
Dilution IHC-P (5 µg/ml)
Additional Information
Gene ID 9320
Other Names E3 ubiquitin-protein ligase TRIP12, 6.3.2.-, E3 ubiquitin-protein ligase for Arf, ULF, Thyroid receptor-interacting protein 12, TR-interacting protein 12, TRIP-12, TRIP12, KIAA0045, ULF
Reconstitution & Storage Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted.
PrecautionsTRIP12 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name TRIP12
Synonyms KIAA0045, ULF
Function E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.
Cellular Location Nucleus, nucleoplasm
Volume 50 µl
Citations (0)

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Background

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.

References

Chen D.,et al.Nature 464:624-627(2010).
Nomura N.,et al.DNA Res. 1:223-229(1994).
Hillier L.W.,et al.Nature 434:724-731(2005).
Lee J.W.,et al.Mol. Endocrinol. 9:243-254(1995).
Olsen J.V.,et al.Cell 127:635-648(2006).

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$ 395.00
Cat# ALS15172
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