DDIT3, Polyclonal Antibody

DNA damage-inducible transcript 3 protein; DDIT-3; C/EBP zeta; C/EBP-homologous protein; CHOP; C/EBP-homologous protein 10; CHOP-10; CCAAT/enhancer-binding protein homologous protein; Growth arrest and DNA damage-inducible protein GADD153; DDIT3; CHOP; CHOP10; GADD153

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit Ig

Rabbit

This DDIT3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 120-149 amino acids from the C-terminal region of human DDIT3.

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Vial Concentration: 0.42 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-DDIT3 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

This gene encodes a member of the CCAAT/enhancer-binding
protein (C/EBP) family of transcription factors. The protein
functions as a dominant-negative inhibitor by forming heterodimers
with other C/EBP members, such as C/EBP and LAP (liver activator
protein), and preventing their DNA binding activity. The protein is
implicated in adipogenesis and erythropoiesis, is activated by
endoplasmic reticulum stress, and promotes apoptosis. Fusion of
this gene and FUS on chromosome 16 or EWSR1 on chromosome 22
induced by translocation generates chimeric proteins in myxoid
liposarcomas or Ewing sarcoma. Multiple alternatively spliced
transcript variants encoding two isoforms with different length
have been identified.

Developmental Biology; Metabolism; Signal Transduction

Western Blot (WB), ELISA (EIA), Flow Cytometry (FC/FACS), Immunofluorescence (IF)

IF~~1:10~50
WB~~1:1000

Fluorescent image of Hela cell stained with DDIT3 Antibody (C-term A135). Hela cells were fixed with 4% PFA (20 min), permeabilized with Triton X-100 (0.1%, 10 min), then incubated with DDIT3 primary antibody (1:25, 1 h at 37 degree). For secondary antibody, Alexa Fluor 488 conjugated donkey anti-rabbit antibody (green) was used (1:400, 50 min at 37 degree).Cytoplasmic actin was counterstained with Alexa Fluor 555 (red) conjugated Phalloidin (7units/ml, 1 h at 37 degree). DDIT3 immunoreactivity is localized to Cytoplasm significantly.

DDIT3 Antibody (C-term A135) western blot analysis in mouse testis tissue lysates (35ug/lane).This demonstrates the DDIT3 antibody detected the DDIT3 protein (arrow).

DDIT3 Antibody (C-term A135) flow cytometric analysis of 293 cells (right histogram) compared to a negative control cell (left histogram).FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.

19175

DNA-damage-inducible transcript 3

DNA damage-inducible transcript 3 protein

DNA damage-inducible transcript 3 protein

CHOP; CHOP10; GADD153; DDIT-3; CHOP; CHOP-10  [Similar Products]

DDIT3_HUMAN

This gene encodes a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors. The protein functions as a dominant-negative inhibitor by forming heterodimers with other C/EBP members, such as C/EBP and LAP (liver activator protein), and preventing their DNA binding activity. The protein is implicated in adipogenesis and erythropoiesis, is activated by endoplasmic reticulum stress, and promotes apoptosis. Fusion of this gene and FUS on chromosome 16 or EWSR1 on chromosome 22 induced by translocation generates chimeric proteins in myxoid liposarcomas or Ewing sarcoma. Multiple alternatively spliced transcript variants encoding two isoforms with different length have been identified. [provided by RefSeq, Aug 2010]

CHOP: a transcriptional-regulatory protein of the bZIP family. Inhibits the DNA-binding activity of C/EBP and LAP by forming heterodimers that cannot bind DNA. May play an important role in melanoma progression. CK2-mediated phosphorylation inhibits its transcriptional activity. Up-regulates IL-6 transcription by trapping negative regulating NF-IL6 isoform.

Protein type: Transcription factor; Oncoprotein; DNA-binding; Autophagy

Chromosomal Location of Human Ortholog: 12q13.1-q13.2

Cellular Component: nucleoplasm; late endosome; cytosol; nucleus

Molecular Function: protein binding; leucine zipper domain binding; DNA binding; protein heterodimerization activity; transcription factor binding; transcription corepressor activity; transcription factor activity

Biological Process: regulation of transcription in response to stress; proteasomal ubiquitin-dependent protein catabolic process; Wnt receptor signaling pathway; negative regulation of protein kinase B signaling cascade; unfolded protein response; negative regulation of transcription factor activity; positive regulation of transcription, DNA-dependent; negative regulation of transcription from RNA polymerase II promoter; blood vessel maturation; mRNA transcription from RNA polymerase II promoter; response to unfolded protein; response to starvation; positive regulation of interleukin-8 production; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; regulation of transcription, DNA-dependent; cell redox homeostasis; positive regulation of neuron apoptosis; release of sequestered calcium ion into cytosol; positive regulation of transcription from RNA polymerase II promoter; negative regulation of myoblast differentiation; cell cycle arrest; negative regulation of transcription, DNA-dependent; inhibition of CREB transcription factor; response to DNA damage stimulus; ER overload response

Disease: Myxoid Liposarcoma

Park, S.H., et al. J. Immunol. 185(9):5522-5530(2010)
Goodall, J.C., et al. Proc. Natl. Acad. Sci. U.S.A. 107(41):17698-17703(2010)
Zhang, H.M., et al. J. Virol. 84(17):8446-8459(2010)
Cazanave, S.C., et al. Am. J. Physiol. Gastrointest. Liver Physiol. 299 (1), G236-G243 (2010) :
Wang, Y.L., et al. J. Exp. Clin. Cancer Res. 29, 54 (2010) :

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