CDK9 (C12F7) Rabbit mAb (PE Conjugate) #32038
- F
Supporting Data
| REACTIVITY | H M R Hm Mk B Dg |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit |
Application Key:
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Hm-Hamster
- Mk-Monkey
- B-Bovine
- Dg-Dog
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
CDK9 (C12F7) Rabbit mAb (PE Conjugate) detects endogenous levels of total CDK9 protein, both 42 kDa and 55 kDa isoforms.
Species Reactivity:
Human, Mouse, Rat, Hamster, Monkey, Bovine, Dog
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human CDK9.
Background
P-TEFb is a general transcription factor that regulates transcription elongation through phosphorylation of the C-terminal tail domain (CTD) of RNA polymerase II (RNAP II). The P-TEFb complex is composed of a catalytic subunit, CDK9, and its regulatory cyclin partner, which can be cyclin T1, T2a, T2b or K (reviewed in 1,2). P-TEFb is recruited by the HIV Tat protein to allow transcriptional elongation, and subsequent replication of the viral genome. Inhibition of P-TEFb function therefore has potential for HIV therapy. CDK9 exists as two isoforms, an abundant 42 kDa isoform, and a less abundant 55 kDa isoform, which contains an amino-terminal extension (3). The two forms likely have distinct purposes based on differential expression during lymphocyte activation (4,5) and on their localization within the nucleus (5).
Cyclin dependent kinases (CDKs) are activated in part by cyclin binding and by phosphorylation of a conserved threonine in the T-loop domain. Phosphorylation of CDK9 at the T-loop Thr186 by an unidentified nuclear kinase may be important in P-TEFb activation (6) and regulation of HIV transcription (7). Acetylation of CDK9 at Lys44 affects its ability to phosphorylate the RNAPII CTD (8).
- Rice, A.P. and Herrmann, C.H. (2003) Curr HIV Res 1, 395-404.
- De Falco, G. and Giordano, A. (2002) Cancer Biol Ther 1, 342-7.
- Shore, S.M. et al. (2003) Gene 307, 175-82.
- Shore, S.M. et al. (2005) Gene 350, 51-8.
- Liu, H. and Herrmann, C.H. (2005) J Cell Physiol 203, 251-60.
- Chen, R. et al. (2004) J Biol Chem 279, 4153-60.
- Ammosova, T. et al. (2005) Retrovirology 2, 47.
- Fu, J. et al. (2007) Mol Cell Biol 27, 4641-51.
- De Falco, G. and Giordano, A. Cancer Biol Ther 1, 342-7.
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