|Application ||WB, IHC-P, E|
|Dilution||ELISA (1 µg/ml), IHC-P (20 µg/ml), WB (1 µg/ml)|
|Other Names||Derlin-3, Degradation in endoplasmic reticulum protein 3, DERtrin-3, Der1-like protein 3, DERL3, C22orf14, DER3, LLN2|
|Target/Specificity||synthetic peptide corresponding to N-terminal residues of human DERL3 (Derlin-3)|
|Reconstitution & Storage||+4°C or -20°C, Avoid repeated freezing and thawing.|
|Precautions||Derlin-3 / DERL3 Antibody (N-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded glycoproteins (PubMed:16449189, PubMed:22607976). May be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908).|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
|Tissue Location||Unlike DERL1 and DERL2, restricted to several tissues. Expressed at high levels in placenta, pancreas, spleen and small intestine.|
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Provided below are standard protocols that you may find useful for product applications.
Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate.
Shimizu N.,et al.Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Collins J.E.,et al.Genome Biol. 5:R84.1-R84.11(2004).
Dunham I.,et al.Nature 402:489-495(1999).
Oda Y.,et al.J. Cell Biol. 172:383-393(2006).
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