Datasheet

Biological Description

Specificity	CHOP Antibody [K6F19] detects endogenous levels of total CHOP protein.
Background	CHOP (C/EBP homologous protein), also known as GADD153 or DDIT3, is a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors central to cellular stress responses, particularly the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. CHOP is a 169-amino-acid protein featuring an N-terminal transcriptional activation domain and a C-terminal basic-leucine zipper (bZIP) domain that mediates DNA binding and dimerization. The bZIP domain allows heterodimerization with other C/EBPs and CREB/ATF family members, but proline and glycine substitutions in its basic region disrupt DNA binding at canonical C/EBP sites, enabling CHOP to function as a dominant-negative regulator of C/EBP-mediated transcription. CHOP is strongly upregulated under ER stress and promotes apoptosis by regulating target genes such as GADD34 and Ero1-Lα. GADD34 facilitates eIF2α dephosphorylation, restoring protein synthesis, while Ero1-Lα increases oxidative stress within the ER, together contributing to programmed cell death. Additionally, phosphorylation of CHOP at serine residues 79 and 82 by p38 MAP kinase enhances its transcriptional activity and is necessary for CHOP-induced apoptosis, particularly in macrophages.

Specificity

CHOP Antibody [K6F19] detects endogenous levels of total CHOP protein.

Background

CHOP (C/EBP homologous protein), also known as GADD153 or DDIT3, is a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors central to cellular stress responses, particularly the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. CHOP is a 169-amino-acid protein featuring an N-terminal transcriptional activation domain and a C-terminal basic-leucine zipper (bZIP) domain that mediates DNA binding and dimerization. The bZIP domain allows heterodimerization with other C/EBPs and CREB/ATF family members, but proline and glycine substitutions in its basic region disrupt DNA binding at canonical C/EBP sites, enabling CHOP to function as a dominant-negative regulator of C/EBP-mediated transcription. CHOP is strongly upregulated under ER stress and promotes apoptosis by regulating target genes such as GADD34 and Ero1-Lα. GADD34 facilitates eIF2α dephosphorylation, restoring protein synthesis, while Ero1-Lα increases oxidative stress within the ER, together contributing to programmed cell death. Additionally, phosphorylation of CHOP at serine residues 79 and 82 by p38 MAP kinase enhances its transcriptional activity and is necessary for CHOP-induced apoptosis, particularly in macrophages.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:50

Reactivity

Mouse

Source

Rabbit Monoclonal Antibody

MW

27 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/14685163/
https://pubmed.ncbi.nlm.nih.gov/29230213/

CHOP Antibody [K6F19]

Biological Description

Usage Information

References

Application Data