| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | 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 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | A 21 residue synthetic peptide (amino acids 192-212) based on the bovine KDEL receptor and the peptide coupled to KLH |
| Isotype | |
| Product Type | |
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| Target |
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.
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.
Cite this product varies by variant:
- SMC-129D — Size: 100 ug: KDEL Receptor Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D, RRID: AB_2132188)
- SMC-129D-A390 — Size: 100 ug: KDEL Receptor Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-A390, RRID: AB_2698143)
- SMC-129D-A488 — Size: 100 ug: KDEL Receptor Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-A488, RRID: AB_2698144)
- SMC-129D-A594 — Size: 100 ug: KDEL Receptor Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-A594, RRID: AB_2698146)
- SMC-129D-APC — Size: 100 ug: KDEL Receptor Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-APC, RRID: AB_2698152)
- SMC-129D-BI — Size: 100 ug: KDEL Receptor Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-BI, RRID: AB_2698153)
- SMC-129D-FITC — Size: 100 ug: KDEL Receptor Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-FITC, RRID: AB_2698154)
- SMC-129D-HRP — Size: 100 ug: KDEL Receptor Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-HRP, RRID: AB_2698155)
- SMC-129D-PCP — Size: 100 ug: KDEL Receptor Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-PCP, RRID: AB_2698157)
- SMC-129D-RPE — Size: 100 ug: KDEL Receptor Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129D-RPE, RRID: AB_2698158)
- SMC-129S — Size: 12 ug: KDEL Receptor Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-129S, RRID: AB_2132188)
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
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