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乙酰化赖氨酸抗体
点击次数:870
价格:¥2875
更新日期:2025/11/7 5:34:47
生 产 地:中国大陆
产品型号:100ug/ml
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详细内容
| Catalog Number | Pack Size | |
| ICP0380 | 100 µg |
Product Description: This pan-specific antibody is affinity purified using acetyllysine affinity chromatography. It recognizes proteins with acetyllysine residues. The product has been utilized for proteomic studies of the protein acetylation, immunoaffinity charomatography separation and isolation of the acetylated protein and peptides from protease-digesting proteins of the whole cells.
Species: Rabbit
Formulation: 250 µg/mL antibody stored in PBS, 50% glycerol
Storage & Stability: Store product at -20 ℃. Three years
from date of shipping.
Immunogen: Acetylated KLH conjugates
Purification: The antibody was purified on acetyl-lysine agarose
Specificity: The antibody recognizes proteins acetylated on lysine residues.
Application: ELISA,WB,IP,IHC,IF.
Tested: Acetylated histone, acetylated BSA, and acetylated MBP, no reaction to the non-acetylated proteins
Scientific Description: DNA transcription can not take place unless DNA is unwound from the nucleosomes. The cell unwinds the DNA by acetylation of lysine residues within the proteins. It has been suggested that acetylation of non-histones proteins (e.g., transcription factors) and histones may be involved. Acetylation of the proteins may result in signal transduction within the chromatic domains.
| Storage & Stability | Product is stable for several weeks at 4°C. For extended storage, aliquot content and store product at –20ºC. Avoid cycles of freezing and thawing. Expiration date is three years from date of shipping if properly stored. |
| Publications |
1. Mol. Cell, 2006. Volume 23, Issue 4, Pages 607-618 2. Mol. Cell. Biol., 2007. p. 1280-1295, Vol. 27, No. 4 3. Curr. Protoc. Protein Sci., 2008. 54:14.11.1-14.11.17 4.Molecular & Cellular Proteomics, 2009. 8:215-225 5.Cell, 2009. Volume 137, Issue 3, Pages 560-570 6.J. Mol.Biol.2009. 392:33-47 7.Cell, 2009. Volume 140, Issue 2, Pages 257-267 8.Science, 2009.325, 834-40 9.The Journal of Immunology, 2010. 185, 3960-3969 10.PROTEOMICS, 2010. 10, 1029–1039 11.Cell, 2010. 140, 257-267 12.Molecular Cell, 2010. 39, 247-258 13.Nature, 2010. 467, 218-224 14.Biochem and Biophys Res Comm., 2011. 404,68⁻⁷3 15.European Journal of Cell Biol. 2011. 90, 128-135 16.Plant Physiology, 2011. 155, 1779-1790 17.Nucleic Acids Research, 201. 1–19 18.Molecular Cell, 2011. 42, 426-437 19.Anal. Chem., 2011. 83, 3623–3626 20.The American Diabetes Association, 2013. Doi: 10.2337/db12-1650 21.The Journal of Lipid Research. 2012. 54: 1864 -1876 22.The Journal of Biological Chemistry. 2012. 287: 32307-32311 23.Journal of Proteomics. 2012. 79: 60⁻⁷1 24.Molecular & Cellular Proteomics. 2012. 11: 202-214 25.The Journal of Biological Chemistry. 2012. doi: 10.1074/jbc.M112.382226 26.Molecular and Cellular Biology. 2012. 32 (14): 2823-2836 27.PLoS Genetics. 2012. 8 (9): e1002948 28.Genes & Dev. 2012. 26: 1473-1485 29.Cell. 2012. 150 (3): 620-632 30.Nature (London). 2012. 482 (7384): 251-255 31.Nature Medicine. 2012. 18 (1): 159-165 32.Molecular Systems Biology. 2012. 8: 571 33.Mol. Cell. Biol., 2013. 33 (6): 1114-1123 34.J. Proteome Res., 2013. 12 (9): 3952-3968 35.Proteomics, 2013. 13 (15): 2278-2282 36.The Journal of Biological Chemistry, 2013, 288: 26209-26219 37.The Journal of Biological Chemistry, 2013. 288: 15537-15546 38.PLoS ONE, 2013. 8 (7): e67513 39.The American Society for Biochemistry and Molecular Biology, Inc., 2013. 1-24. 40.Mol. Cell. Biol., 2013. 33 (19): 3864-3878 41.Nature, 2013. 496: 110-113 42.J. Biol. Chem., 2013. Doi: 10.1074/jbc.M113.495549 43.Molecular Microbiology, 2013. 89 (4): 660-675 |


