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Lead Time
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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). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex.; (Microbial infection) Required early in hepatitis C virus (HCV) infection to initiate RNA replication, and later in the infection to support infectious virus production.
Gene References into Functions
Erlin-1 and the related erlin-2 were found to selectively bind cholesterol. Knockdown of the proteins by RNAi in cultured cells resulted in high levels of cholesterol and fatty acid biosynthesis in the presence of cholesterol sufficiency. PMID: 24217618
Here we show that the multimeric ER proteins erlins-1 and -2 are additional sterol regulatory element binding protein regulators. PMID: 24217618
Our findings suggest ERLIN1-CHUK-CWF19L1 variants are associated with early stage of fatty liver accumulation to hepatic inflammation. PMID: 23477746
Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. PMID: 16835267
Results suggest that this novel SPFH1/2 complex is a recognition factor that targets IP(3)Rs and perhaps other substrates for ERAD. PMID: 19240031
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. PMID: 19751772
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane.
Protein Families
Band 7/mec-2 family
Tissue Specificity
Expressed in heart, placenta, liver, kidney, pancreas, prostate, testis, ovary and small intestine.