Cell Signaling Technology

Product Pathways - Protein Stability

HIP2 (D27C4) Rabbit mAb #8226

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk (B) Endogenous 25 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

HIP2 (D27C4) Rabbit mAb recognizes endogenous levels of total HIP2 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu161 of human HIP2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using HIP2 (D27C4) Rabbit mAb.

Background

Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3 (1).

Huntingtin-interacting protein-2 (HIP2), also known as E2-25K, is a member of the E2 protein family that is highly expressed in the brain and catalyzes multiubiquitin chain synthesis via Lys48 of ubiquitin (2). E2-25K is reportedly involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-β, huntingtin, and MHC-heavy chain proteins (3-6). Recent studies have also implicated HIP2 in the control of apoptosis and cell-cycle progression through its ability to regulate the stability of Smac/Diablo and cyclin B1 (7,8).

  1. Hershko, A. (1988) J. Biol. Chem. 263, 15237-15240.
  2. Chen, Z. and Pickart, C.M. (1990) J Biol Chem 265, 21835-42.
  3. Song, S. et al. (2003) Mol Cell 12, 553-63.
  4. de Pril, R. et al. (2007) Mol Cell Neurosci 34, 10-9.
  5. Flierman, D. et al. (2006) Proc Natl Acad Sci USA 103, 11589-94.
  6. Kalchman, M.A. et al. (1996) J Biol Chem 271, 19385-94.
  7. Bae, Y. et al. (2010) Biochem Biophys Res Commun 397, 718-23.
  8. Bae, Y. et al. (2010) FEBS Lett 584, 4505-10.

Application References

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

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