|Other Names||ER lumen protein-retaining receptor 1, KDEL endoplasmic reticulum protein retention receptor 1, KDEL receptor 1, Putative MAPK-activating protein PM23, KDELR1, ERD21|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Required for the retention of luminal endoplasmic reticulum resident proteins via vesicular recycling. This receptor recognizes the C-terminal K-D-E-L motif. COPI-coated transport intermediates, either in the form of round vesicles or as tubular processes, mediate retrograde traffic of the KDEL receptor-ligand complexes. Also required for normal vesicular traffic through the Golgi.|
|Cellular Location||Cytoplasmic vesicle, COPI-coated vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane|
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Provided below are standard protocols that you may find useful for product applications.
Retention of resident soluble proteins in the lumen of theendoplasmic reticulum (ER) is achieved in both yeast and animalcells by their continual retrieval from the cis-Golgi, or apre-Golgi compartment. Sorting of these proteins is dependent on aC-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) inanimal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. Thisprocess is mediated by a receptor that recognizes, and binds thetetrapeptide-containing protein, and returns it to the ER. Inyeast, the sorting receptor encoded by a single gene, ERD2, whichis a seven-transmembrane protein. Unlike yeast, several humanhomologs of the ERD2 gene, constituting the KDEL receptor genefamily, have been described. The protein encoded by this gene wasthe first member of the family to be identified, and it encodes aprotein structurally and functionally similar to the yeast ERD2gene product.
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Breuza, L., et al. J. Biol. Chem. 279(45):47242-47253(2004)Bard, F., et al. J. Biol. Chem. 278(47):46601-46606(2003)Yamamoto, K., et al. J. Biol. Chem. 278(36):34525-34532(2003)Matsuda, A., et al. Oncogene 22(21):3307-3318(2003)
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