| 货号 | 9956T |
| 描述 | The ER Stress Sampler Kit contains reagents to investigate ER stress within the cell. The kit contains enough primary and secondary antibodies to perform four Western blot experiments per primary antibody. |
| 目标/特异性 | Each antibody in the ER Stress Antibody Sampler Kit detects endogenous levels of its target protein. |
| 供应商 | CST |
| 背景 | 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). |
| 存放说明 | -20C |
| 参考文献 | 1 . Harding, H.P. et al. (1999) Nature 397, 271-4. 2 . Bergeron, J.J. et al. (1994) Trends Biochem. Sci. 19, 124-128. 3 . Cabibbo, A. et al. (2000) J. Biol. Chem. 275, 4827-4833. 4 . Nikawa, J. and Yamashita, S. (1992) Mol Microbiol 6, 1441-6. 5 . Williams, D.B. (2006) J Cell Sci 119, 615-23. 6 . Frand, A.R. and Kaiser, C.A. (1998) Mol. Cell 1, 161-170. 7 . Cox, J.S. et al. (1993) Cell 73, 1197-206. 8 . Shen, J. and Prywes, R. (2004) J. Biol. Chem. 279, 43046-43051. 9 . Harding, H. et al. (2000) Mol. Cell 5, 897-904. 10 . Ellgaard, L. and Ruddock, L.W. (2005) EMBO Rep 6, 28-32. 11 . Mori, K. et al. (1993) Cell 74, 743-56. 12 . Lee, K. et al. (2002) Genes Dev 16, 452-66. 13 . Kaufman, R.J. et al. (2002) Nat Rev Mol Cell Biol 3, 411-21. 14 . Kohno, K. et al. (1993) Mol Cell Biol 13, 877-90. 15 . Zinszner, H. et al. (1998) Genes Dev 12, 982-95. |
Flow cytometric analysis of A204 cells using BiP (C50B12) Rabbit mAb (blue) compared to concentration-matched Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (red). Anti-rabbit IgG (H+L), F(ab)2 Fragment (Alexa Fluor® 488 Conjugate) #4412 was used as a secondary antibody. | |
Immunohistochemical analysis of paraffin-embedded mouse spleen using PDI (C81H6) Rabbit mAb. | |
Chromatin immunoprecipitations were performed with cross-linked chromatin from 4 x 106 MEF wild-type cells treated with tunicamycin (2ug/ml) overnight, and 1 µl of CHOP (L63F7) Mouse mAb or 2 µl of Normal Rabbit IgG #2729 using SimpleChIP® Enzymatic Chromatin IP Kit (Magnetic Beads) #9003. The enriched DNA was quantified by real-time PCR using SimpleChIP® Mouse ATF-3 Intron 1 Primers #13059, mouse CHOP promoter primers, and SimpleChIP® Mouse RPL30 Intron 2 Primers #7015. The amount of immunoprecipitated DNA in each sample is represented as signal relative to the total amount of input chromatin, which is equivalent to one. | |
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using PERK (D11A8) Rabbit mAb. | |
Western blot analysis of extracts from various cell lines using PERK (D11A8) Rabbit mAb. | |
Western blot analysis of extracts from various cell lines using PERK (D11A8) Rabbit mAb #5683. 对多个细胞系提取物使用PERK (D11A8) Rabbit mAb兔单抗 #5683进行Western blot分析。 | |
Confocal immunofluorescent analysis of NIH/3T3 cells using PDI (C81H6) Rabbit mAb (green) and β-Actin (8H10D10) Mouse mAb #3700 (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye). | |
Western blot analysis of extracts from various cell types using PDI (C81H6) Rabbit mAb #3501. 对多个细胞系使用PDI (C81H6) Rabbit mAb兔单抗 #3501进行Western blot分析。 | |
Immunohistochemical analysis of paraffin-embedded human lymphoma using PDI (C81H6) Rabbit mAb. | |
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using PDI (C81H6) Rabbit mAb. | |
Western blot analysis of extracts from various cell types using PDI (C81H6) Rabbit mAb. | |
Western blot analysis of extracts from C6 and A204 cells, untreated or treated with thapsigargin (300 nM) or tunicamycin (24 μg/ml), using CHOP (L63F7) Mouse mAb #2895. 对未处理或者thapsigargin (300 nM)或tunicamycin (24 ug/ml)处理过的C6和A204细胞使用CHOP (L63F7) Mouse mAb #2895进行Western blot分析。 | |
Western blot analysis of extracts from PANC1, HepG2 and A204 cells using Calnexin (C5C9) Rabbit mAb #2679. 对PANC1、HepG2和A204细胞抽提液使用Calnexin (C5C9) Rabbit mAb兔单抗 #2679进行Western blot分析。 | |
Western blot analysis of extracts from C6 and A-204 cells, untreated or treated with thapsigargin (300 nM, 2 hours) or tunicamycin (24 μg/ml, 2 hours), using CHOP (L63F7) Mouse mAb. | |
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Calnexin (C5C9) Rabbit mAb in the presence of control peptide (left) or antigen-specific peptide (right). |
