DHX9 Antibody #70998
- WB
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 145 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
DHX9 Antibody recognizes endogenous levels of total DHX9 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala25 of human DHX9 protein. Antibodies are purified by peptide affinity chromatography.
Background
DExH-box helicase 9 (DHX9), also known as nuclear DNA helicase II or RNA helicase A, is a protein involved in unwinding DNA and RNA by using NTP (1). DHX9 can translocate in the 3’ to 5’ direction and can utilize all dNTPs or rNTPs, and contributes to pre-mRNA splicing (2,3). Essential for embryo development, DHX9 plays roles in many biological processes, including DNA replication, self-renewal, dosage compensation, and neuronal development (4-7). DHX9 is a critical regulator of abnormal DNA secondary structures (8). It is recruited by TDRD3 to R-loops, where it can unwind and resolve them to prevent DNA damage (9-12). DHX9 plays a central role in the formation and resolution of R-loops (8-11). It also can bind to G-quadruplexes and inverted-repeat Alu elements, suppressing formation of circular RNAs (9,13). BRCA1 is recruited to RNA by DHX9 to promote homologous recombination (14). Furthermore, DHX9 has been shown to be upregulated in various cancer types and can also play a role in viral replication (15-17).
- Zhang, S. and Grosse, F. (1994) Biochemistry 33, 3906-12.
- Lee, C.G. and Hurwitz, J. (1992) J Biol Chem 267, 4398-407.
- Zhang, S. et al. (1999) J Cell Sci 112 (Pt 7), 1055-64.
- Friedemann, J. et al. (2005) J Biol Chem 280, 31303-13.
- Närvä, E. et al. (2012) Stem Cells 30, 452-60.
- Kuroda, M.I. et al. (1991) Cell 66, 935-47.
- Hoekstra, E.J. et al. (2013) PLoS One 8, e53122.
- Jain, A. et al. (2013) Nucleic Acids Res 41, 10345-57.
- Chakraborty, P. and Grosse, F. (2011) DNA Repair (Amst) 10, 654-65.
- Chakraborty, P. et al. (2018) Nat Commun 9, 4346.
- Cristini, A. et al. (2018) Cell Rep 23, 1891-1905.
- Yuan, W. et al. (2021) Nucleic Acids Res 49, 8573-8591.
- Aktaş, T. et al. (2017) Nature 544, 115-119.
- Chakraborty, P. and Hiom, K. (2021) Nat Commun 12, 4126.
- Shi, F. et al. (2021) J Clin Lab Anal 35, e24052.
- Xiao, L. et al. (2022) J Cancer 13, 102-111.
- Guo, F. and Xing, L. (2021) Virus Res 291, 198206.
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