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ERdj5 is a member of the proteostasis network that regulates rod opsin biogenesis and supports a role for disulfide bond formation/reduction in rod opsin biogenesis and disease.
ERdj5, by binding to Sel1L (show SEL1L Proteins), triggers BiP (show GDF10 Proteins)-Cholera toxin interaction proximal to the Hrd1 (show SYVN1 Proteins) complex; postulate this scenario enables the Hrd1 (show SYVN1 Proteins)-associated retrotranslocation machinery to capture the toxin efficiently once the toxin is released from BiP (show GDF10 Proteins)
ERdj5 acts as the endoplasmic reticulum reductase, both preparing misfolded proteins for degradation and catalyzing the folding of proteins that form obligatory non-native disulfides.
ERdj5 is a ubiquitous protein localized in the ER and is particularly abundant in secretory cells. Its transcription is induced during ER stress, suggesting potential roles for ERdj5 in protein folding and translocation across the ER membrane.
JPDI may have roles in folding of some proteins in the ER, chaperoning by BiP (show GDF10 Proteins) and formation of proper disulfide bonds
The organization of the functional motifs of hMTHr suggests that the protein might be a member of a molecular chaperone (show HSP90AA1 Proteins) family.
ERdj4 and ERdj5 promote turnover of misfolded SP-C and this activity is dependent on their ability to stimulate BiP ATPase activity.
study found that an endoplasmic reticulum (ER) protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins & accelerated ER-associated degradation through its physical and functional associations with EDEM (show EDEM1 Proteins) & BiP (show GDF10 Proteins)
ERdj5 decreases neuroblastoma (show ARHGEF16 Proteins) cell survival by down-regulating the UPR, raising the possibility that this protein could be a target for anti-tumor approaches.
study identified the redox partners of ERdj5 from the mouse epididymis; findings show that ERdj5 interacted with two of the identified proteins via formation of intermolecular disulfide bond
Data suggest that ERdj5 contributes to ER protein quality control in the salivary gland.
JPDI may have roles in folding of some proteins in the ER, chaperoning by BiP (show HSPA5 Proteins) and formation of proper disulfide bonds
study found that an endoplasmic reticulum (ER) protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins & accelerated ER-associated degradation through its physical and functional associations with EDEM (show EDEM1 Proteins) & BiP (show HSPA5 Proteins)
This gene encodes an endoplasmic reticulum co-chaperone which is part of the endoplasmic reticulum-associated degradation complex involved in recognizing and degrading misfolded proteins. The encoded protein reduces incorrect disulfide bonds in misfolded glycoproteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
ER-resident protein ERdj5
, J-domain-containing protein disulfide isomerase-like protein
, dnaJ homolog subfamily C member 10
, protein disulfide isomerase family A, member 19
, endoplasmic reticulum DnaJ-PDI fusion protein 1
, j domain-containing PDI-like protein
, j domain-containing protein disulfide isomerase-like protein
, DnaJ homolog
, DnaJ (Hsp40) homolog, subfamily C, member 10