Product: DDIT3/CHOP mouse monoclonal Antibody
Catalog: BF8018
Description: Mouse monoclonal antibody to DDIT3/CHOP
Application: WB IHC
Reactivity: Mouse, Rat
Mol.Wt.: 19~30kD; 19kD(Calculated).
Uniprot: P35638

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Product Info

Source:
Mouse
Application:
IHC 1:50-1:200, WB 1:500-1:2000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Mouse,Rat
Clonality:
Monoclonal [AFfirm8018]
Specificity:
DDIT3 Antibody detects endogenous levels of total DDIT3.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

C/EBP homologous protein; C/EBP Homology Protein; C/EBP zeta; C/EBP-homologous protein 10; C/EBP-homologous protein; CCAAT/enhancer binding protein homologous protein; CEBPZ; CHOP 10; CHOP; CHOP-10; CHOP10; DDIT 3; DDIT-3; Ddit3; DDIT3_HUMAN; DNA Damage Inducible Transcript 3; DNA damage-inducible transcript 3 protein; GADD 153; GADD153; Growth Arrest and DNA Damage Inducible Protein 153; Growth arrest and DNA damage inducible protein GADD153; Growth arrest and DNA damage-inducible protein GADD153; MGC4154;

Immunogens

Immunogen:

A synthesized peptide derived from human DDIT3, corresponding to a region within N-terminal amino acids.

Uniprot:
Gene(ID):
Description:
CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).
Sequence:
MAAESLPFSFGTLSSWELEAWYEDLQEVLSSDENGGTYVSPPGNEEEESKIFTTLDPASLAWLTEEEPEPAEVTSTSQSPHSPDSSQSSLAQEEEEEDQGRTRKRKQSGHSPARAGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRRALIDRMVNLHQA

PTMs - P35638 As Substrate

Site PTM Type Enzyme
S14 Phosphorylation P68400 (CSNK2A1)
S15 Phosphorylation P68400 (CSNK2A1)
S30 Phosphorylation P68400 (CSNK2A1)
S31 Phosphorylation P68400 (CSNK2A1)
S49 Phosphorylation
T54 Phosphorylation
T64 Phosphorylation
S79 Phosphorylation Q16539 (MAPK14)
S82 Phosphorylation Q16539 (MAPK14)

Research Backgrounds

Function:

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: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response.

PTMs:

Ubiquitinated, leading to its degradation by the proteasome.

Phosphorylation at serine residues by MAPK14 enhances its transcriptional activation activity while phosphorylation at serine residues by CK2 inhibits its transcriptional activation activity.

Subcellular Location:

Cytoplasm. Nucleus.
Note: Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Heterodimer. Interacts with TCF7L2/TCF4, EP300/P300, HDAC1, HDAC5 and HDAC6. Interacts with TRIB3 which blocks its association with EP300/P300. Interacts with FOXO3, CEBPB and ATF4. Interacts with isoform AltDDIT3 of DDIT3.

Family&Domains:

The N-terminal region is necessary for its proteasomal degradation, transcriptional activity and interaction with EP300/P300.

Belongs to the bZIP family.

Research Fields

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Cancers: Overview > Transcriptional misregulation in cancer.

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