DERL2 / Derlin-2 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
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Primary Accession | Q9GZP9 |
Other Accession | 51009 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | 27567 Da |
Dilution | IHC-P (5 µg/ml), WB (1:1000), |
Gene ID | 51009 |
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Other Names | DERL2, Carcinoma related, CGI-101, DER2, Derlin 2, Derlin-2, F-LANa, F-LAN-1, FLANa, Der1-like protein 2, DERtrin-2 |
Target/Specificity | DERL2 / Derlin-2 |
Reconstitution & Storage | PBS, pH 7.2, 50% glycerol. Store at -20°C. |
Precautions | DERL2 / Derlin-2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | DERL2 (HGNC:17943) |
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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 misfolded glycoproteins (PubMed:16186509, PubMed:16449189). May also 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 | Ubiquitous. Overexpressed in various hepatocarcinomas. |
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Background
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. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation.
References
Ying H.,et al.Biochem. Biophys. Res. Commun. 286:394-400(2001).
Lai C.-H.,et al.Genome Res. 10:703-713(2000).
Zhang W.,et al.Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Lilley B.N.,et al.Nature 429:834-840(2004).
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