JDP2 Antibody (3C1): sc-517133

JDP2 Antibody (3C1) is a mouse monoclonal IgG2a kappa light chain antibody that detects JDP2 protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-JDP2 antibody (3C1) is available as the non-conjugated form. The c-Jun dimerization protein (JDP) 2 plays a crucial role in regulating gene expression by binding to cAMP-response elements (CRE) as either a homodimer or a heterodimer with ATF-2 and c-Jun, thereby repressing CRE-dependent transcription. This regulatory function is vital for various cellular processes, including differentiation and response to external stimuli. JDP2 is phosphorylated at Thr 138 by c-Jun N-terminal kinase, which can influence activity and interactions. JDP2 features a basic leucine zipper (bZIP) domain essential for DNA-binding capabilities, allowing interaction with the DNA-binding domain of the progesterone receptor (PR) in mammalian cells. This interaction enhances PR transcriptional activity by facilitating association with coactivators such as CREB-binding protein (CBP) and p300 CBP-associated factor (PCAF). JDP2 expression in PR-targeted tissues underscores importance in PR-mediated signaling pathways. JDP2 is implicated in F9 embryonal carcinoma cell differentiation, recruiting histone deacetylase 3 (HDAC3) to the c-jun promoter, thus regulating the transcriptional landscape during differentiation. The gene encoding human JDP2 is located on chromosome 14q24.2, highlighting evolutionary conservation and potential significance in developmental biology and disease.

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JDP2 Antibody (3C1) References:

1. Identification of mouse Jun dimerization protein 2 as a novel repressor of ATF-2.  |  Jin, C., et al. 2001. FEBS Lett. 489: 34-41. PMID: 11231009
2. AP-1 repressor protein JDP-2: inhibition of UV-mediated apoptosis through p53 down-regulation.  |  Piu, F., et al. 2001. Mol Cell Biol. 21: 3012-24. PMID: 11287607
3. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells.  |  Jin, C., et al. 2002. Mol Cell Biol. 22: 4815-26. PMID: 12052888
4. Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator.  |  Wardell, SE., et al. 2002. Mol Cell Biol. 22: 5451-66. PMID: 12101239