KDEL Receptor Antibody, Clone KR-10: Biotin

KDEL receptors are key components of the endoplasmic reticulum (ER) protein quality control system, essential for maintaining cellular homeostasis. These receptors recognize and retrieve ER-resident proteins bearing the KDEL (Lys-Asp-Glu-Leu) C-terminal motif, preventing their loss during vesicular transport to the Golgi apparatus. Variants of the KDEL sequence also contribute to ER retention, reflecting the system’s adaptability. In mammalian cells, three highly conserved KDEL receptor isoforms are localized to the cis-Golgi and ER-Golgi intermediate compartments. Functionally, KDEL receptors interact with ARF1 GTPase-activating proteins (GAPs), facilitating COPI-dependent retrograde vesicle transport. This retrieval mechanism is critical for sustaining ER function, especially under conditions of proteotoxic stress. In the context of neurodegenerative diseases—such as Alzheimer’s, Parkinson’s, and ALS—chronic ER stress and impaired protein folding are central pathological features. Dysregulation of KDEL receptor function can disrupt the unfolded protein response (UPR), exacerbate protein misfolding, and contribute to neuronal dysfunction and degeneration. Moreover, the KDEL receptor shares significant sequence identity with the yeast Erd2p, underscoring its evolutionary conservation and fundamental role in ER homeostasis. As interest grows in targeting ER stress pathways for therapeutic intervention, the KDEL receptor is emerging as a promising molecular target in neurodegenerative disease research.

KDELR1, KDEL receptor 1, KDEL endoplasmic reticulum protein retention receptor 1, ER lumen protein-retaining receptor 1, ERD2, ERD2.1, ERD21, KDEL R1, PM23, HDEL

1 µg/ml was sufficient for detection of KDEL receptor in 20 µg monkey Vero cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:AP as the secondary.

1. Whiteman P., and Handford P.A. (2003) Hum Mol Genet 12(7): 727-737. 2. Forthoffer N., et al. (2002) J Bioenerg Biomemb 34(3): 209-219. 3. Aoe T., et al. (1997) EMBO J. 16: 7305-7316. 4. Tang B.L., Wong S.H, Qi X.L. Low S.H., and Hong W. (1993) J. Cell Biol. 120: 325-328. 5. Lewis M.J. and Pelham H.R. (1990) Nature 348: 162-163. 6. Spurger L. (2002). Endoplasmic reticulum: Structure and function. University of Texas Medical Branch. Retrieved September 13, 2006, from http://cellbio.utmb.edu/cellbio/rer1.htm

1. Whiteman P., and Handford P.A. (2003) Hum Mol Genet 12 (7) : 727-737. 2. Forthoffer N., et al. (2002) J Bioenerg Biomemb 34 (3) : 209-219. 3. Aoe T., et al. (1997) EMBO J. 16: 7305-7316. 4. Tang B.L., Wong S.H, Qi X.L. Low S.H., and Hong W. (1993) J. Cell Biol. 120: 325-328. 5. Lewis M.J. and Pelham H.R. (1990) Nature 348: 162-163. 6. Spurger L. (2002) . Endoplasmic reticulum: Structure and function. University of Texas Medical Branch. Retrieved September 13, 2006, from http://cellbio.utmb.edu/cellbio/rer1.htm

Human | Mouse | Rat | Bovine | Monkey | Hamster | Rabbit | Pig | Sheep | Dog | Chicken | Fruit Fly (Drosophila melanogaster) | African clawed frog (Xenopus laevis)