Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, which is a seven-transmembrane protein. Unlike yeast, several human homologs of the ERD2 gene, constituting the KDEL receptor gene family, have been described. The protein encoded by this gene was the first member of the family to be identified, and it encodes a protein structurally and functionally similar to the yeast ERD2 gene product.
ER lumen protein retaining receptor 1 antibody
ERD 2 antibody
KDEL (Lys Asp Glu Leu) endoplasmic reticulum protein retention receptor 1 antibody
ab96720 at 1/20,000 dilution staining KDEL Receptor in a human kidney tissue section by Immunohistochemistry (Formalin/PFA fixed paraffin-embedded sections). Secondary antibody was biotinylated Goat anti-mouse. Picture at 400X magnification.