Key Specifications Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|M, R||WB, ICC, IP||Rb||Affinity Purified||Polyclonal Antibody|
|Presentation||Purified rabbit polyclonal in buffer containing 155 mM NaCl, 50 mM Tris-HCl pH 7.4, with 0.05% sodium azide and 10% glycerol.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Stable for 1 year at 2-8°C from date of receipt.
Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
|Material Size||200 µL|
|Anti-ERLIN1/SPFH1, C-terminus -Q2564187||Q2564187|
|Reference overview||Pub Med ID|
|An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors.|
Pearce, MM; Wormer, DB; Wilkens, S; Wojcikiewicz, RJ
The Journal of biological chemistry 284 10433-45 2009
How endoplasmic reticulum (ER) proteins that are substrates for the ER-associated degradation (ERAD) pathway are recognized for polyubiquitination and proteasomal degradation is largely unresolved. Inositol 1,4,5-trisphosphate receptors (IP(3)Rs) form tetrameric calcium channels in ER membranes, whose primary role is to control the release of ER calcium stores, but whose levels are also regulated, in an activation-dependent manner, by the ERAD pathway. Here we report that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric approximately 2 MDa complex that binds to IP(3)R tetramers immediately after their activation and is required for their processing. The complex is ring-shaped (diameter approximately 250A(),) and RNA interference-mediated depletion of SPFH1 and SPFH2 blocks IP(3)R polyubiquitination and degradation. We propose that this novel SPFH1/2 complex is a recognition factor that targets IP(3)Rs and perhaps other substrates for ERAD.
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