DNA damage-inducible transcript 3 protein is a protein in humans that is encoded by DDIT3 gene. Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription
The following DDIT3 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.
DDIT3 Antibodies for Homo sapiens (Human)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA006589GA01HU | DDIT3 Antibody |
Human,Mouse,Rat | ELISA,WB |
CSB-PA071811 | DDIT3 Antibody |
Human,Mouse,Rat | ELISA, WB, IHC, IF |
CSB-PA799326 | Phospho-DDIT3 (Ser30) Antibody |
Human,Mouse | ELISA,WB |
CSB-PA001639 | DDIT3 Antibody |
Human,Mouse,Rat | WB, IHC, IF, ELISA |
CSB-PA001640 | DDIT3 Antibody |
Human,Mouse | WB, IHC, IF, ELISA |
CSB-PA007699 | Phospho-DDIT3 (S30) Antibody |
Human,Mouse | WB, IHC, IF, ELISA |
CSB-PA006589LA01HU | DDIT3 Antibody |
Human | ELISA, IHC, IF |
CSB-PA006589LB01HU | DDIT3 Antibody, HRP conjugated |
Human | ELISA |
DDIT3 Proteins for Homo sapiens (Human)
Code | Product Name | Source |
---|---|---|
CSB-YP006589HU CSB-EP006589HU CSB-BP006589HU CSB-MP006589HU CSB-EP006589HU-B |
Recombinant Human DNA damage-inducible transcript 3 protein(DDIT3) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
DDIT3 Proteins for Mus musculus (Mouse)
Code | Product Name | Source |
---|---|---|
CSB-YP006589MO CSB-EP006589MO CSB-BP006589MO CSB-MP006589MO CSB-EP006589MO-B |
Recombinant Mouse DNA damage-inducible transcript 3 protein(Ddit3) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
DDIT3 Proteins for Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Code | Product Name | Source |
---|---|---|
CSB-YP006589DXU CSB-EP006589DXU CSB-BP006589DXU CSB-MP006589DXU CSB-EP006589DXU-B |
Recombinant Cricetulus griseus DNA damage-inducible transcript 3 protein(DDIT3) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
DDIT3 Proteins for Bos taurus (Bovine)
Code | Product Name | Source |
---|---|---|
CSB-YP606584BO CSB-EP606584BO CSB-BP606584BO CSB-MP606584BO CSB-EP606584BO-B |
Recombinant Bovine DNA damage-inducible transcript 3 protein(DDIT3) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
DDIT3 Proteins for Rattus norvegicus (Rat)
Code | Product Name | Source |
---|---|---|
CSB-YP737096RA CSB-EP737096RA CSB-BP737096RA CSB-MP737096RA CSB-EP737096RA-B |
Recombinant Rat DNA damage-inducible transcript 3 protein(Ddit3) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
DNA damage-inducible transcript 3 (DDIT3), also called C/EBP homologous protein (CHOP), is an endoplasmic reticulum (ER) stress-inducible protein that belongs to a member of the CCAAT/enhancer-binding protein (C/EBP) family of DNA-binding transcription factors [1][2]. DDIT3/CHOP functions as a multifunctional transcription factor that contributes to cellular functions, including apoptosis, autophagy, inflammation, cell differentiation, and proliferation. DDIT3/CHOP possesses N-terminal transcriptional activation/repression domains necessary for its proteasomal degradation and a C-terminal basic-leucine zipper (bZIP) domain, including a basic region for DNA binding and a leucine zipper motif for dimerization [3]. A serine/threonine-rich motif in the transactivation domain of DDIT3/CHOP can be recognized by speckle-type POZ protein (SPOP), which triggers DDIT3/CHOP degradation via the ubiquitin-proteasome pathway [4]. TRB3 antagonized p300 binding to CHOP via its N-terminal domain [5]. Degradation of CHOP protein through the N-terminal domain was inhibited by treatment with trichostatin A (TSA) [5]. During ER stress, CHOP is mainly induced via activation of the PERK (ER-localized kinase double-stranded RNA-activated protein kinase (PKR)-like ER kinase) through the downstream phosphorylation of a translation initiation factor, eukaryotic initiation factor 2α (eIF2α), and induction of a transcription factor, activation transcription factor 4 (ATF4) [6]. Apoptosis ensues by ATF4-CHOP-mediated induction of several pro-apoptotic genes and suppression of the synthesis of anti-apoptotic Bcl-2 proteins [7]. Also, Oyadomari, S. and Mori, M. demonstrated that CHOP-mediated apoptosis during ER stress is involved in diseases with ER stress-dependent cell death, such as neurodegenerative disease and/or type I diabetes [8]. During amino acid limitation and ER stress, CHOP binds to the promoters of a set of autophagy genes [9]. WafaB'chir and his colleagues showed that during the first 6 h of starvation, CHOP upregulates numerous autophagy genes but is not involved in the first steps of the autophagic process. When the amino acid starvation is prolonged (16–48 h), CHOP exhibits a dual role in both inducing apoptosis and limiting autophagy through the transcriptional control of specific genes [10]. CHOP is also implicated in adipogenesis and erythropoiesis.
[1] Fornace, A. J., Nebert, D. et al. Mammalian genes coordinately regulated by growth arrest signals and DNA-damaging agents [J]. Mol. Cell. Biol. 1989, 9, 4196–4203.
[2] Lekstrom-Himes J. and Xanthopoulos K. G. Biological role of the CCAAT/enhancer-binding protein family of transcription factors [J]. J. Biol. Chem. 1998, 273, 28545–28548.
[3] Ubeda M, Wang XZ, et al. Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element [J]. Molecular and Cellular Biology. 1996, 16 (4): 1479–89.
[4] Zhang P, Gao K, et al. Destruction of DDIT3/CHOP protein by wild-type SPOP but not prostate cancer-associated mutants [J]. Hum Mutat (2014) 35(9):1142–51.
[5] Nobumichi Ohoka, Takayuki Hattori, et al. Critical and Functional Regulation of CHOP (C/EBP Homologous Protein) through the N-terminal Portion [J]. The Journal of Biological Chemistry 2007, 282, 35687-35694.
[6] Harding, H. P., Novoa, I., et al. Regulated translation initiation controls stress-induced gene expression in mammalian ce[J]. Mol. Cell 200o, 6, 1099–1108.
[7] W Rozpedek, D Pytel, et al. The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress [J]. Curr Mol Med, 2016, 16 (6), 533-44.
[8] Oyadomari, S., and Mori, M. Roles of CHOP/GADD153 in endoplasmic reticulum stress[J]. Cell Death Differ. 2004, 11, 381–389.
[9] B’Chir W, Maurin AC, et al. The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression [J]. Nucleic Acids Res (2013) 41(16):7683–99.
[10] WafaB'chir, Cédric Chaveroux, et al. Dual role for CHOP in the crosstalk between autophagy and apoptosis to determine cell fate in response to amino acid deprivation [J]. Volume 26, Issue 7, July 2014, Pages 1385-1391.