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Human Polyclonal DERL2 Primary Antibody for IHC - ABIN965991
Lilley, Ploegh: A membrane protein required for dislocation of misfolded proteins from the ER. in Nature 2004
Show all 3 Pubmed References
specific silencing of Derlin-2, p97 (show EIF4G2 Antibodies) and HRD1 (show SYVN1 Antibodies) by shRNAs increases steady state levels of proinsulin (show INS Antibodies). these ERAD constituents are critically involved in proinsulin (show INS Antibodies) degradation and may therefore also play a role in subsequent antigen generation.
derlin2 functions with HRD1 (show SYVN1 Antibodies) 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 Antibodies) and p97 (show EIF4G2 Antibodies) in the process of degrading misfolded glycoproteins.
Whole-body deletion of derlin-2 leads to perinatal lethality and skeletal abnormalities.
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
, carcinoma related
, degradation in endoplasmic reticulum protein 2
, der1-like protein 2
, derlin 2