BACH1 (E4E7B) Rabbit mAb #33059
- WB
- IP
- ChIP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 100 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:10 - 1:50 |
| Immunoprecipitation | 1:100 |
| Chromatin IP | 1:100 |
| Chromatin IP-seq | 1:100 |
Storage
Protocol
Specificity / Sensitivity
BACH1 (E4E7B) Rabbit mAb recognizes endogenous levels of total BACH1 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the central region of human BACH1 protein.
Background
BTB and CNC homology 1 (BACH1) is a basic leucine zipper transcription factor that is widely expressed in mammalian tissues (1). Through its roles in both transcriptional activation and repression, BACH1 regulates a wide range of cellular processes, including senescence, heme homeostasis, oxidative stress response, and the cell cycle (2-5). In competition with NRF2, BACH1 regulates ferroptosis; BACH1 promotes the process while NRF2 inhibits it (6,7). BACH1 heterodimerizes with Maf proteins (8). These heterodimers bind to Maf recognition elements at the promoters of oxidative stress response genes, such as heme oxygenase-1 (HMOX1) and NAD(P)H:quinone oxidoreductase 1 (NQO1) (9,10). As a transcriptional repressor, BACH1 recruits nuclear receptor corepressor 1 (NCoR1) as well as histone deacetylase 1 (HDAC1) (3). BACH1 has recently been implicated as a driver of cancer metastasis and is a potential therapeutic target in breast and lung cancer (11-13).
- Zhang, X. et al. (2018) Oxid Med Cell Longev 2018, 1347969.
- Oyake, T. et al. (1996) Mol Cell Biol 16, 6083-95.
- Dohi, Y. et al. (2008) Nat Struct Mol Biol 15, 1246-54.
- Ogawa, K. et al. (2001) EMBO J 20, 2835-43.
- Warnatz, H.J. et al. (2011) J Biol Chem 286, 23521-32.
- Nishizawa, H. et al. (2023) FEBS J 290, 1688-1704.
- Nishizawa, H. et al. (2020) J Biol Chem 295, 69-82.
- Igarashi, K. et al. (2021) J Biol Chem 297, 101032.
- Sun, J. et al. (2002) EMBO J 21, 5216-24.
- Dhakshinamoorthy, S. et al. (2005) J Biol Chem 280, 16891-900.
- Lee, J. et al. (2019) Nature 568, 254-258.
- Wiel, C. et al. (2019) Cell 178, 330-345.e22.
- Padilla, J. and Lee, J. (2021) Cells 10, 634.
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