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Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs)..
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Here we show that the multimeric ER proteins erlins-1 and -2 are additional sterol regulatory element binding protein (show CNBP Proteins) regulators.
Our findings suggest ERLIN1-CHUK-CWF19L1 variants are associated with early stage of fatty liver accumulation to hepatic inflammation.
Erlin-1 and erlin-2 (show ERLIN2 Proteins) are novel members of the prohibitin (show PHB Proteins) family of proteins that define lipid-raft-like domains of the ER.
Results suggest that this novel SPFH1/2 complex is a recognition factor that targets IP(3)Rs and perhaps other substrates for ERAD.
m3 receptor-expressing HeLa cells are a valuable system for studying IP(3) receptor ERAD, and suggest that the SPFH1/2 complex is a factor that selectively mediates the ERAD of activated IP(3) receptors.
2 MDa erlin1/2 complex is composed of an assemblage of lower-order hetero-oligomers, probably heterotrimers, linked together by assembly domain hydrophobic residues.
Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs).
, SPFH domain-containing protein 1
, endoplasmic reticulum lipid raft-associated protein 1
, stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1
, ER lipid raft associated 1
, SPFH domain family, member 1
, Band_7 23-211 Keo4 (Interim) similar to C.elegans protein C42C1.9
, ER lipid raft-associated 1
, protein KE04 homolog
, Endoplasmic reticulum lipid raft-associated protein 2-B
, SPFH domain-containing protein 2-B
, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2-B