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The tetrapeptide KDEL, located at the carboxy-terminal sequences of luminal proteins, is a retrieval motif essential for the precise sorting of these proteins along the secretory pathway. KDEL proteins perform essential functions in the endoplasmic reticulum (ER) related to protein folding as well as assembly. The localization of chaperones and other soluble proteins to the ER is achieved by their continuous retrieval from post-ER compartments by the KDEL receptor (Erd2p), which is a membrane protein localized in the Golgi apparatus.
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Flow cytometry analysis of 106 Jurkat cells stained using KDEL mAb (10C3), DyLight 488™.
| Regulatory Status |
RUO – Research Use Only |
|---|
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| Alternative Name | Endoplasmin, Tra1, Hsp90B1, Gp96 |
|---|---|
| Application | Electron microscopy, ICC, IF, IHC (PS), IP, WB |
| Host | Rat |
| Isotype | IgG2a |
| Species Reactivity | Bovine, Chicken, Dog, Guinea pig, Hamster, Human, Monkey, Mouse, Porcine, Rabbit, Rat, Sheep, Xenopus |
| Alternative Name | HspA5, Hsp70-5, Heat shock 70 kDa protein 5 |
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| Purity | ≥80% (SDS-PAGE; Western blot) |
| Source | Produced in E. coli. |
| Alternative Name | Tra1, Tumor rejection antigen 1, Hsp90B1, Gp96, Heat shock protein 90 kDa beta member 1, Endoplasmin |
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| Purity | ≥90% (SDS-PAGE; Western blot) |
| Source | Produced in Sf21 insect cells. Produced in a baculovirus expression system. |