ASXL2 (E6Z3X) Rabbit mAb #71257
- WB
Supporting Data
| REACTIVITY | H Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 210 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
ASXL2 (E6Z3X) Rabbit mAb recognizes endogenous levels of total ASXL2 protein.
Species Reactivity:
Human, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala640 of human ASXL2 protein.
Background
Additional sex combs-like protein 2 (ASXL2) is a polycomb-associated protein that interacts with polycomb repressive complex 2 (PRC2), which contains the histone methyltransferase EZH2 and functions to mono-, di-, and tri-methylate histone H3 on lysine 27. These histone marks are associated with transcriptional repression (1). In addition, ASXL2 interacts with BRCA1-associated protein 1 (BAP1), the catalytic subunit of the polycomb repressive deubiquitinase complex (PR-DUB), which functions to de-ubiquitinate histone H2A at lysine 119 and activate transcription (2). ASXL2 functions as a transcriptional regulator of adipogenesis, acting to induce peroxisome proliferator-activated receptor gamma (PPARG) adipocyte differentiation, whereas its paralog ASXL1 functions to inhibit PPARG activity (3). ASXL2 is critical for animal viability and growth, as ASXL2 knockout mice experience partial embryonic lethality, premature death, axial skeletal abnormalities, and reduced bone mineral density (4,5). ASXL2 also plays a role in cancer, where ASXL2 truncation mutations are found in pancreatic, breast, and castration-resistant prostate cancers, albeit infrequently (6-9). ASXL2 is also frequently mutated in acute myeloid leukemia patients with t(8;21)/RUNX1-RUNX1T1 chromosomal translocations, and these mutations correlate with a 36% incidence of relapse (10).
- Abdel-Wahab, O. et al. (2012) Cancer Cell 22, 180-93.
- Daou, S. et al. (2015) J Biol Chem 290, 28643-63.
- Park, U.H. et al. (2011) J Biol Chem 286, 1354-63.
- Baskind, H.A. et al. (2009) PLoS One 4, e4750.
- Farber, C.R. et al. (2011) PLoS Genet 7, e1002038.
- Katoh, M. (2013) Br J Cancer 109, 299-306.
- Jones, S. et al. (2008) Science 321, 1801-6.
- Stephens, P.J. et al. (2012) Nature 486, 400-4.
- Grasso, C.S. et al. (2012) Nature 487, 239-43.
- Micol, J.B. et al. (2014) Blood 124, 1445-9.
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