DDX3 (D19B4) Rabbit mAbProduct information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Cell Cycle / Checkpoint
DDX3 (D19B4) Rabbit mAb #8192
|8192S||100 µl (10 western blots)||---||In Stock||---|
|8192||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||75||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
DDX3 (D19B4) Rabbit mAb recognizes endogenous levels of total DDX3 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human DDX3 protein.
The DEAD box family of RNA helicases is characterized in part by a common D-E-A-D amino acid motif. The family is composed of a growing number of proteins found in a wide range of organisms from bacteria to mammals. DEAD helicases have distinct biological functions in RNA metabolism and ribonucleoprotein (RNP) processing (reviewed in 1,2).
DDX3 is a DEAD box family RNA helicase with diverse cellular functions. DDX3 is required for nuclear export of HIV-1 viral transcripts, possibly in a complex with the viral Rev protein and host cofactor CRM1 (3). DDX3 is required for hepatitis C virus (HCV) RNA replication (4) and its expression is downregulated in hepatitis B virus (HBV) associated hepatocellular carcinoma (HCC) (5).
Recent evidence suggests that DDX3 functions as a tumor suppressor protein. Its expression inhibits tumor cell colony formation and increases expression of the cdk inhibitor p21 Waf1/Cip1. Low DDX3 expression has been shown in HCC (5,6), and aberrant subcellular localization occurs in many squamous cell carcinomas (6). Reduced DDX3 expression in cultured cells causes a diminished dependence on serum for cell proliferation and changes in cyclin D1 and p21 Waf1/Cip1 expression (5).
DDX3 is phosphorylated at Thr204 and Thr323 by the mitotic cyclin dependent kinase, cyclin B/cdc2. This phosphorylation is thought to cause a loss of DDX3 function and a concomitant repression of ribosome biogenesis and translation in mitosis (7).
- Rocak, S. and Linder, P. (2004) Nat Rev Mol Cell Biol 5, 232-41.
- Linder, P. (2006) Nucleic Acids Res 34, 4168-80.
- Yedavalli, V.S. et al. (2004) Cell 119, 381-92.
- Ariumi, Y. et al. (2007) J Virol 81, 13922-6.
- Chang, P.C. et al. (2006) Oncogene 25, 1991-2003.
- Chao, C.H. et al. (2006) Cancer Res 66, 6579-88.
- Sekiguchi, T. et al. (2007) Biochem Biophys Res Commun 356, 668-73.
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