KDEL Antibody, Clone 2C1: Biotin

The endoplasmic reticulum (ER) plays a central role in protein folding, quality control, and trafficking within eukaryotic cells. A key mechanism for retaining essential chaperones and folding enzymes within the ER involves the C-terminal KDEL sequence (Lys-Asp-Glu-Leu), a highly conserved ER retention motif. Proteins such as GRP78, GRP94, and protein disulfide isomerase (PDI) —critical for maintaining proteostasis—contain the KDEL motif, which ensures their retrieval from the Golgi apparatus back to the ER. This retention system is vital for sustaining ER function under both physiological and stress conditions. In the context of neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, and ALS, chronic ER stress and impaired protein homeostasis are hallmark features. The KDEL retrieval system is increasingly recognized as a key modulator of the unfolded protein response (UPR), a cellular defense mechanism activated by misfolded proteins. Dysregulation of KDEL-containing chaperones can exacerbate protein aggregation, neuronal dysfunction, and cell death. Moreover, experimental evidence suggests that enhancing KDEL-mediated retention can reduce aberrant protein secretion and improve ER stress resilience, offering potential therapeutic avenues. As such, the KDEL motif and its associated retrieval machinery are emerging as critical components in the study of neurodegeneration and cellular stress adaptation.

A 1:1000 dilution of SMC-539 was sufficient for detection of KDEL in 10 µg of HeLa cell lysates by ECL immunoblot analysis using goat anti-mouse IgG:HRP as the secondary antibody.