| Product Includes | Product # | Quantity | Mol. Wt | Isotype/Source |
|---|---|---|---|---|
| BiP (C50B12) Rabbit mAb | 3177 | 20 µl | 78 kDa | Rabbit IgG |
| Calnexin (C5C9) Rabbit mAb | 2679 | 20 µl | 90 kDa | Rabbit IgG |
| Ero1-Lα Antibody | 3264 | 20 µl | 60 kDa | Rabbit |
| IRE1α (14C10) Rabbit mAb | 3294 | 20 µl | 130 kDa | Rabbit IgG |
| PDI (C81H6) Rabbit mAb | 3501 | 20 µl | 57 kDa | Rabbit |
| CHOP (L63F7) Mouse mAb | 2895 | 20 µl | 27 kDa | Mouse IgG2a |
| PERK (D11A8) Rabbit mAb | 5683 | 20 µl | 140 kDa | Rabbit IgG |
| Anti-rabbit IgG, HRP-linked Antibody | 7074 | 100 µl | Goat | |
| Anti-mouse IgG, HRP-linked Antibody | 7076 | 100 µl | Horse |
Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.
Description
The ER Stress Sampler Kit contains reagents to investigate ER stress within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.
Storage
Background
Secretory and transmembrane proteins are synthesized on polysomes and translocate into the endoplasmic reticulum (ER) where they are often modified by the formation of disulfide bonds, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperone proteins including calnexin, BiP and protein disulfide isomerase (PDI). Calnexin is an ER membrane, calcium-binding protein that retains newly synthesized glycoproteins inside the ER to ensure proper folding and quality control (1,2). Irregular protein folding within the ER increases BiP synthesis, which binds misfolded proteins to prevent them from forming aggregates and to assist them to refold properly (3).
PDI catalyzes the formation and isomerization of disulfide bonds required for a protein to reach its native state (4). Studies have found that the resident ER protein endoplasmic oxidoreductin-1 (Ero1) provides oxidizing potential to the ER in Saccharomyces cerevisiae (5). Ero1-Lα is an ER membrane-associated N-glycoprotein that promotes oxidative protein folding (6). Disruptions of ER homeostasis leads to the accumulation of unfolded proteins. The ER has developed an adaptive mechanism called the unfolded protein response (UPR) to counteract compromised protein folding (7). This is regulated by proteins such as the membrane-bound transcription factor protease site 2 (MBTPS2) and the serine/threonine kinase IRE1 (8-12). The PERK eIF2α kinase is an ER resident transmembrane protein that couples ER stress signals to translation inhibition. ER stress increases PERK activity, which phosphorylates eIF2α to reduce protein translation. PERK activation during ER stress correlates with autophosphorylation of its cytoplasmic kinase domain (13,14). Phosphorylation of PERK at Thr980 can serve as a marker for its activation status.
During ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (15).
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Background References
Trademarks and Patents
Limited Uses
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