IRE1p Antibody

IRE1p Antibody: Accumulation of malfolded proteins in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR) and the upregulation of the ER molecular chaperones GRP78 and GRP 94. These proteins are normally bound to ER transmembrane proteins such as IRE1p and ATF6 but ER stress causes their dissociation. This allows IRE1p, a serine-threonine protein kinase to transduce the unfolded protein signal from the ER to the nucleus. IRE1p also has an endoribonuclease activity that is required to splice X-box binding protein (XBP1) mRNA converting it to a potent UPR transcriptional activation. Depletion of IRE1p through the expression of a dominant negative form of IRE1p has no effect on transfected cells, but cell death via apoptosis occurs under stress conditions that cause unfolded proteins to accumulate in the ER. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.

IRE1p antibody can be stored at 4˚ C for three months and -20˚ C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Little E, Ramakrishnan M, Roy B, et al. The glucose-regulated proteins (GRP78 and GRP94) : functions, gene regulation, and applications. Crit. Rev. Eukaryot. Gene Expr.1994; 4:1-18.

Bertolotti A, Zhang Y, Hendershot LM, et al. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol.2000; 2:326-32.

Shen J, Chen X, Hendershot L, et al. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell2002; 3:99-111.