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Whole-body deletion of derlin-2 leads to perinatal lethality and skeletal abnormalities.
specific silencing of Derlin-2, p97 (show EIF4G2 Proteins) and HRD1 (show SYVN1 Proteins) by shRNAs increases steady state levels of proinsulin (show INS Proteins). these ERAD constituents are critically involved in proinsulin (show INS Proteins) degradation and may therefore also play a role in subsequent antigen generation.
derlin2 functions with HRD1 (show SYVN1 Proteins) in ERAD of certain substrates independent of their glycosylation status.
Derlin-2 forms a robust multiprotein complex with the p97 AAA ATPase as well as the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex, and participates in the degradation of proteins from the ER.
Findings indicate that Derlin-2 provides the missing link between EDEM (show EDEM1 Proteins) and p97 (show EIF4G2 Proteins) in the process of degrading misfolded glycoproteins.
Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. DERL2 is involved in the degradation of misfolded glycoproteins in the ER (Oda et al., 2006
Der1-like domain family, member 2
, derlin 2
, carcinoma related
, degradation in endoplasmic reticulum protein 2
, der1-like protein 2