抗IRE1 alpha [p Ser724]抗体 | Anti-IRE1 alpha [p Ser724] Antibody

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	Biological Strategies Validation. Western Blot: IRE1 alpha [p Ser724] Antibody [NB100-2323] - Western blot of anti-IRE1 alpha (pSer724) using Lot AN and AO of NB100-2323. HeLa cells were treated (+) or untreated (-) with 10 mM DTT for 60 min to activate the UPR. Total protein was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% BSA in TBST. The membrane was probed with 2.0 ug/ml antibody in 5% BSA, and detected with an anti-rabbit HRP secondary antibody using chemiluminecence.
	Biological Strategies Validation. Western Blot: IRE1 alpha [p Ser724] Antibody [NB100-2323] - Detection in Min6 cells which were treated with different concentrations of glucose for 3 hours prior to lysates preparation.
	Genetic Strategies Validation. Western Blot: IRE1 alpha [p Ser724] Antibody [NB100-2323] - Analysis using HRP conjugate of NB100-2323. Detection of phosphorylated IRE-1 alpha using NB100-2323. Lane 1: COS-7 untransfected Lane 2: COS-7 expressing wild-type IRE1 alpha Lane 3: COS-7 expressing kinase-dead IRE1 alpha.

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Background

Unfolded protein response (UPR) signaling, a mechanism used by eukaryotic cells to cope ER stress. It is initiated by three ER-localized protein sensors: PERK (PKR-like ER kinase), ATF (activating transcription factor 6), and IRE1 alpha (inositol-requiring enzyme 1 alpha). UPR-responsive genes's transcriptional activation is regulated by ATF6 and IRE1-XBP1 pathways, and UPR serves three important functions: inhibition of protein translation to restore normal cell functions; activation of signaling to increase production of molecular chaperones involved in protein folding; and activation of signaling that leads to targeting of misfolded proteins in ER for ubiquitination and subsequent degradation; or when ER-stress is not relieved, UPR leads to apoptosis. Localized as a single-pass type I membrane protein in ER membrane, IRE1 alpha is ubiquitously expressed with high levels observed in pancreatic tissue. It undergoes autophosphorylation and gets ADP-ribosylated by PARP16 upon ER stress, which increases its kinase as well as endonuclease activities. IRE1 alpha senses unfolded proteins in the ER lumen via its N-terminal domain which leads to enzyme auto-activation and thereafter, the active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent UPR transcriptional activator. IRE1 alpha inactivation in mice has been shown to result in widespread developmental defects, leading to intra-gestational embryonic lethality and ER stress mediated cell death is responsible for several pathologies.

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