Rabbit polyclonal antibody to ERdj3 (K66)

Members of the heat shock protein 40 (HSP 40) family of proteins all contain a highly conserved J domain that associates with HSP 70 and regulates the function of HSP 70 by activating its adenosine triphosphatase activity. ERdj3, an HSP 40 chaperone, is expressed in the ER lumen, where it interacts with BiP, a molecule involved in retrotranslocating proteins out of the ER. ERdj3 also associates with several other protein substrates, including unfolded light chains, a nonsecreted Ig light chain mutant and a VSV~G ts045 mutant. Shiga toxin (Stx) is a bacterial tool that enzymatically inactivates the 28S rRNA, inhibiting protein synthesis of infected cells. Stx also interacts with ERdj3 and Sec 61 to form a complex through which proteins are retrotranslocated to the cytoplasm. ERdj3 may play a role in the ER quality control system.