Cell Signaling Technology

Product Pathways - DNA Damage

HR6A/HR6B Antibody #4944

Applications Reactivity MW (kDa) Source
W IF-IC F H M R Mk (C) (Dm) (X) (Z) 17 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  C=Chicken  Dm=D. melanogaster  X=Xenopus  Z=Zebra Fish
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

HR6A/HR6B Antibody detects endogenous levels of total HR6A and HR6B proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide (KLH-coupled) corresponding to amino acids at the amino-terminus of human HR6A. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, ME-180, 293 and K562 cells, using HR6A/HR6B Antibody.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of untreated Jurkat cells, using HR6A/HR6B Antibody (blue) compared to a nonspecific negative control antibody (red).

IF-IC

IF-IC

Immunofluorescent analysis of ME-180 cells, using HR6A/HR6B Antibody.


Background

The ubiquitin-conjugating (UBC) enzymes HR6A and HR6B are the mammalian orthologues of the Saccharomyces cerevisiae Rad6 gene products (1). In S. cerevisiae, Rad6 facilitates cell cycle progression and ubiquitinates histone H2B (2,3). In vivo phosphorylation of HR6A Ser120 by cyclin-dependent kinases is thought to be important for the coordination and timing of ubiquitination events involved in cell cycle progression (4). In response to DNA damage, HR6A is known to interact physically with p53 and p14ARF, but knockout mice lacking HR6A or HR6B exhibit normal DNA damage responses (5,6). HR6B knockout males exhibit defective spermatogenesis, while HR6A knockout females fail to produce viable offspring (6).

  1. Koken, M. H. et al. (1991) Proc. Natl. Acad. Sci. USA 88, 8865-8869.
  2. Ellison, K. S. et al. (1991) J. Biol. Chem. 266, 24116-24120.
  3. Robzyk, K. et al. (2000) Science 287, 501-504.
  4. Sarcevic, B. et al. (2002) EMBO J. 21, 2009-2018.
  5. Lyakhovich, A. and Shekhar, M.P. (2003) Mol. Cell. Biol. 23, 2463-2475.
  6. Roest, H. P. et al. (2004) Mol. Cell. Biol. 24, 5485-5495.

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