New England Biolabs Canada

Product Pathways - Chromatin Regulation / Epigenetics

UHRF1 (D6G8E) Rabbit mAb #12387

Item# Description List Price Web Price Qty
12387S UHRF1 (D6G8E) Rabbit mAb - 100 µl $372.00
*On-line ordering is for Canadian customers only. Web pricing is applicable only to orders placed online at
Application Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W Human, Mouse, Rat Endogenous 95 Rabbit IgG

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation

Specificity / Sensitivity

UHRF1 (D6G8E) Rabbit mAb recognizes endogenous levels of total UHRF1 protein. This antibody does not cross-react with UHRF2 protein. This antibody may recognize a non-specific 32 kDa protein in some cell lysates.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val78 of human UHF1 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using UHRF1 (D6G8E) Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa cells, expressing either nontargeting shRNA (HeLa shNT) or shRNA targeting UHRF1 (HeLa shUHRF1), using UHRF1 (D6G8E) Rabbit mAb (upper) or GAPDH (D16H11) XP® Rabbit mAb #5174 (lower).



Immunoprecipitation of UHRF1 from HeLa cell extracts, using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or UHRF1 (D6G8E) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using UHRF1 (D6G8E) Rabbit mAb.


Ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1), also known as Inverted CCAAT box-binding protein of 90 kDa (ICBP90) and Nuclear Zinc Finger Protein NP95 (NP95), is a nuclear protein that was first discovered as a CCAAT box-binding protein that regulates the expression of the Topoisomerase IIα and Rb1 genes (1,2). Later studies have shown that UHRF1 is required for maintenance of CpG DNA methylation, the process of copying pre-existing methylation patterns onto the newly synthesized DNA strand after DNA replication (3-5). UHRF1 localizes primarily with highly methylated pericentromeric heterochromatin and is required for proper structure and function of these regions of the genome (6,7). However, UHRF1 also localizes to euchromatic regions of the genome and functions to negatively regulate the expression of a subset of tumor suppressor genes (2,8,9). The localization and repressive functions of UHRF1 are both mediated by several protein domains, including a ubiquitin-like domain (UBQ), Tudor domain, PHD domain, SET and RING finger-associated (SRA) domain, and a RING finger domain. The SRA domain of UHRF1 binds with high affinity to hemi-methylated DNA and functions to properly target the associated maintenance DNA methyltransferase DNMT1 protein to mediate faithful methylation of the newly synthesized DNA strand (3-5). Additional targeting of UHRF1 to heterochromatin is mediated by the Tudor domain, which binds specifically to tri-methylated lysine 9 of histone H3, a histone mark associated with pericentromeric heterochromatin (10-12). Targeting of UHRF1 to euchromatin is further mediated by the PHD domain, which binds specifically to un-methylated arginine 2 of histone H3, which is commonly associated with euchromatin (13). In addition to recruiting DNMT1, UHRF1 recruits the histone deacetylase 1 (HDAC1) protein to target loci, resulting in deacetylation of histones, and providing an additional mechanism for transcriptional repression (3). Taken together, these studies demonstrate that UHRF1 functions to link DNA methylation and histone modifications to the maintenance of repressive chromatin structures. These functions of UHRF1 are important for proper maintenance of cell growth and proliferation, as research studies have shown UHRF1 over-expression in a number of cancers (breast, lung, colon, and prostate cancer) is associated with increased proliferation and malignancy (9,14-16).

  1. Hopfner, R. et al. (2000) Cancer Res 60, 121-8.
  2. Jeanblanc, M. et al. (2005) Oncogene 24, 7337-45.
  3. Unoki, M. et al. (2004) Oncogene 23, 7601-10.
  4. Sharif, J. et al. (2007) Nature 450, 908-12.
  5. Bostick, M. et al. (2007) Science 317, 1760-4.
  6. Papait, R. et al. (2007) Mol Biol Cell 18, 1098-106.
  7. Papait, R. et al. (2008) Mol Biol Cell 19, 3554-63.
  8. Daskalos, A. et al. (2011) Cancer 117, 1027-37.
  9. Kim, J.K. et al. (2009) Nucleic Acids Res 37, 493-505.
  10. Nady, N. et al. (2011) J Biol Chem 286, 24300-11.
  11. Liu, X. et al. (2013) Nat Commun 4, 1563.
  12. Rothbart, S.B. et al. (2012) Nat Struct Mol Biol 19, 1155-60.
  13. Rajakumara, E. et al. (2011) Mol Cell 43, 275-84.
  14. Babbio, F. et al. (2012) Oncogene 31, 4878-87.
  15. Kofunato, Y. et al. (2012) Oncol Rep 28, 1997-2002.
  16. Unoki, M. et al. (2010) Br J Cancer 103, 217-22.

Application References

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