Acetyl Lysine Antibody

Acetyl Lysine Antibody(ICP0380)

Applications:
ELISA; WB (1:1000); IP; Immunofluorescence; Immunochemistry

Specificity:
The Acetyl Lysine Antibody recognizes proteins acetylated on lysine residues. Tested: acetylated histone, acetylated BSA, and acetylated MBP. No cross-reaction to non-acetylated proteins.

Immunogen:
Acetylated KLH conjugates

Species:
Rabbit

Formulation:
250 μg/mL antibody in PBS, 50% glycerol

Pack Size

Price (USD)

Quantity

Datasheet

Recommended products

Methylated (ε-N) Lysine Antibody

( ICP0501) View Details

Dimethyl (asy) Arginine Antibody

( ICP0810) View Details

Mono-Methyl Arginine Antibody

( ICP0801) View Details

Trimethyl Lysine Antibody

( ICP0601) View Details

Acetyl Lysine Antibody, Mouse Monoclonal

( ICP0390) View Details

Product Description

Acetyl Lysine Antibody (ICP0380) is a pan-specific antibody. It is affinity purified using acetyl-lysine affinity chromatography. By recognizing proteins with acetylated lysine residues, this product can be utilized for proteomic studies of acetylated proteins. It can also isolate acetylated proteins/peptides from protease-digested proteins from whole cells using immunoaffinity chromatographic isolation.
Scientific Description

DNA transcription cannot take place unless DNA is unwound from the nucleosomes. The cell unwinds the DNA by acetylating lysine residues within the proteins. It has been suggested that acetylation of non-histone proteins (e.g., transcription factors) and histones may be involved. Acetylation of these proteins may result in signal transduction within the chromatic domains.
Storage & Stability

Product is stable for several weeks at 4°C. For extended storage, store product at –20ºC. Expiration date is one year from date of shipping if properly stored.
Product Specific References
1. Mol. Cell. Proteomics.2009. 8 (2): 215-225. doi:10.1074/mcp.M800187-MCP200.
2. Eur. J. Cell Biol.2011. 90 (2-3): 128-135. doi:10.1016/j.ejcb.2010.09.004.
3. Nucleic Acids Res. 2011. 39 (14): 5907-5925. doi:10.1093/nar/gkr162.
4. J. Lipid Res.2012. 53 (9): 1864 -1876. doi:10.1194/jlr.M026567.
5. J. Biol. Chem. 2012. 287 (39): 32307-32311. doi:10.1074/jbc.C112.403048.
6. Mol. Cell. Proteomics.2012. 11 (5): 202-214. doi:10.1074/mcp.M112.017707.
7. Mol. Cell. Biol.2012. 32(14): 2823-2836. doi:10.1128/MCB.00496-12.
8. PLoS Genet.2012. 8(9): e1002948. doi:10.1371/journal.pgen.1002948.
9. Genes Dev.2012. 26 (13): 1473-1485. doi:10.1101/gad.193615.112.
10. Nature. 2012. 482(7384): 251-255. doi:10.1038/nature10804.
11. Nature Med.2012. 18(1): 159-165. doi:10.1038/nm.2559.
12. Mol. Syst. Biol.2012. 8 (1): 571. doi:10.1038/msb.2012.4.
13. J. Biol. Chem. 2012. 287(29): 24460-24472. doi:10.1074/jbc.M112.382226.
14. J. Proteomics.2013. 79: 60-71. doi:10.1016/j.jprot.2012.12.001.
15. J. Proteome Res.2013. 12 (9): 3952-3968. doi:10.1021/pr400245k.
16. Mol. Cell. Biol,2013.33 (6): 1114-1123. doi:10.1128/MCB.01044-12.
17. Mol. Cell. Biol.2013. 33 (19): 3864-3878. doi:10.1128/MCB.01495-12.
18. Mol. Microbiol. 2013. 89(4): 660-675. doi:10.1111/mmi.12303.
19. PLoS ONE. 2013. 8(7): e67513. doi:10.1371/journal.pone.0067513.
20. Proteomics. 2013. 13(15): 2278-2282. doi:10.1002/pmic.201200072.
21. J. Biol. Chem. 2013. 288 (22): 15537-15546. doi:10.1074/jbc.M112.430207.
22. J. Biol. Chem.2013. 288 (39): 28116-28125. doi:10.1074/jbc.M113.495549.
23. Journal of Biological Chemistry. 2013. 288(42): 30515-30526. doi: 10.1074/jbc.M113.489716
24. Nature.2013. 496 (7443): 110-113. doi:10.1038/nature12038.
25. Diabetes.2013. 62(10): 3404–3417. doi:10.2337/db12-1650.
26. PLoS Genet. 2014. 10(7): e1004490. doi:10.1371/journal.pgen.1004490.
27. Lipids.2014. 49 (2): 119-131. doi:10.1007/s11745-013-3843-x.
28. PLoS ONE.2014. 9 (4): e94816. doi:10.1371/journal.pone.0094816.
29. J. Biol. Chem.2015. 290 (13): 8469-8481 doi:10.1074/jbc.M114.622696.
30. Mol. Cell. 2015. 59(5): 867-881. doi:10.1016/j.molcel.2015.05.006.
31. J. Biol. Chem. 2015. 290 (38): 23077-23093. doi:10.1074/jbc.M115.649806.
32. Plant Mitochondira: Methods and Protocols. 2015. 1305: 107-121. doi:10.1007/978-1-4939-2639-8_7.
33. Mol. Cell. Proteomics. 2015.14: 2429-2440. doi:10.1074/mcp.O114.047555.
34. Cell Death Differ. 2016. 23 (2): 279–290. doi:10.1038/cdd.2015.96.
35. Cancer Res. 2016. 76(13): 3802-3812. doi:1158/0008-5472.CAN-15-2498.
36. Methods Mol Biol.2016. 1436: 85-94. doi:10.1007/978-1-4939-3667-0_6.
37. mSystems. 2016. 1(3): e00005-16. doi:1128/mSystems.00005-16.
38. J Biol Chem. 2016. 291(10): 5270-5277. doi:1074/jbc.M115.709428.
39. PNAS. 2016. 113(16): 4320-4325. doi:1073/pnas.1519858113.
40. Sci Rep. 2016. 6: 19722. doi:1038/srep19722.
41. PLoS ONE. 2016. 11(9): 1-16. doi: 10.1371/journal.pone.0162528.
42. The Journal of Biological Chemistry. 2016. 291:5270-5277 doi: 10.1074/jbc.M115.709428.
43. Molecular & Cellular Proteomics. 2016. doi: 10.1074/mcp.O116.065219.
44. Histone Deacetylases. 2016. 1436:85-94. doi: 10.1007/978-1-4939-3667-0 6.
45. Cancer Research.2016. 76 (13); 3802-12 doi:10.1158/0008-5472.CAN-15-2498.
46. PLOS One. 2016. 11 (12): 1-20. doi: 10.1371/journal.pone.0168467.
47. American Society for Microbiology. 2016. 1(3): 1-19. doi: 10.1128/mSystems.00005-16.
48. Scientific Reports. 2016. 6:31086: 1-9. doi: 10.1038/srep31086.
49. Scientific Reports. 2016. 6: 36013: 1-14. doi: 10.1038/srep36013.
50. South Dakota State University. 2016. 1-131.
51. CellPress.2016. 167 (4): 985-1000. doi: http://dx.doi.org/10.1016/j.cell.2016.10.016.
52. Cell Death and Differentiation. 2015. 23: 279-290. doi: 10.1038/cdd.2015.96.
53. Oncotarget. 2016. 1-14. doi: 10.18632/oncotarget.12015.
54. Journal of Biological Chemistry. 2016. 1-24. doi: 10.1074/jbc.M116.744532.
55. Journal of Proteomics. 2016. doi: 10.1016/j.jprot.2016.12.006.
56. Molecular Microbiology. 2016. doi:10.1111/mmi.13595.
57. App. Environ. Microbiol. 2016. 83(21): 1183-1195 doi: 10.1128/AEM.03056-15.
58. Journal of Thoracic Disease. 2016. 8(9): 2485-2494. doi: 10.21037/jtd.2016.08.08.
59. EMBO Report. 2016. 17(3): 455-469. doi: 10.15252/embr.201541132
60. Mol Cell Biochem. 2017. 432(7): 7-24.doi: 10.1007/211010-017-2993-1
61. J. Proteom. 2017. 155:63-72.doi: 10.1016/jprot.2016.12.006
62. Curr. Protoc. Protein Sci.2017. 87: 14.11.1-14.11.18. doi: 10.1002/cpps.26
63. Biochimica et Biophysica Acta – Proteins and Proteomics.2018. 1866 (3): 451-463. doi:10.1016/j.bbapap.2017.12.001
64. Nature Communications. 2018. 1039 (9). doi: 10.1038/s41467-018-03422-6
65. Front. Pharmacol.2018. 201 (9). doi: 10.3389/fphar.2018.00201
66. Biochimica et Biophysica Acta – Porteins and Proteomics.2018. 1866 (3): 451-463. doi: 10.1016/j.bbapap.2017.12.001
67. Front. Pharmocal. 2018. 201 (9). doi: 10.3389/fphar.2018.002
68. Nature. 2018. 1039 (9). doi: 10.1038/s41467-018-03422-6
69. Journal of Molecular Medicine. 2018.096 (3-4): 281-299. doi: 10.1007/s00109-017-1616-3
70. Molecular Microbiology.2018. doi: 10.1111/mmi.13979
71. Front. Cell. Infect. Microbiol. 2018. doi: 10.3389/fcimb.2017.00537
72. Nature Communications. 2018. 9(1):3436. doi: 10.1038/s41467-018-05451-7
73. Journal of Biological Chemistry.2019.294(16): 6227-6239. doi: 10.1074/jbc.RA118.006051
74. Nature Communications. 2019. 10. doi:10.1038/s41467-019-09024-0
75. Cancer Cell. 2019. 35(6): 916-931. doi: 10.1016/j.ccell.2019.05.002
76. American Journal of Physiology. 2019. 317(2). doi: 10.1152/ajpendo.00326.2018
77. FEBS Letters. 2019. 594(7). doi: 10.1002/1873-3468.13702
78. EMBO. 2019. 38(18). doi:10.15252/embj.2018100948
79. Cell Reports. 2019. 29(3). doi: 10.1016/j.celrep.2019.09.023
80. British Journal of Pharmacology. 2020. 176. doi: 10.1111/bph.15023
81. Cancers. 2020. 12(1031): 1031. doi:10.3390/cancers12041031
82. Mol. Syst. Biol.. 2020. 16(7): e9464. doi:10.15252/msb.20209464
83. Plant Phys. and Bioc.. 2020. 152: 72-80. doi:10.1016/j.plaphy.2020.04.034
84. MBio. 2020. 11(4): e00650-20. doi:10.1128/mBio.00650-20
85. Viruses. 2020. 12(9): 976. doi:10.3390/v12090976
86. Bioc. Journal. 2020. 477(19): 3885–3896. doi:10.1042/BCJ20200413
87. Journal of Proteomics. 2021: 232. doi: 10.1016/j.prot.2020.104044
88. IUBMB Life. 2021. 73(3): 492-510. doi: 10.1002/iub.2407
89. Cell Reports. 2021. 34(13). doi: 10.1016/j.celrep.2021.108921
90. bioRXiv. 2021. 2021.04.21.440833. doi: 10.1101/2021.04.21.440833
91. Plant Physiology and Biochemistry. 2021: 152, 72-80. doi: 10.1016/j.plaphy.2020.04.034
92. PLOS Genetics. 2021. 17(7): e1009459. doi: 10.1371/journal.pgen.1009459
93. Acta Pharmacologica Sinica. 2021. doi: 10.1038/s41401-020-00563-7
94. The Plant Journal. 2021. doi: 10.1111/tpj.15555
95. Cancer Communications. 2021. 1-19. doi: 10.1002/cac2.12221
96. Journal of Biological Chemistry. 2022. 298(2):101538 doi: 10.1016/j.jbc.2021.101538
97. Structure. 2022. 80(9). 1224-1232 doi: 10.1016/j.str.2022.05.020
98. Insect Biochemistry and Molecular Biology. 2023. 162. 104015 doi: 10.1016/j.ibmb.2023.104015
99. Nucleic Acids Research. 2023. 51(11). 5565-5583 doi: 10.1093/nar/gkad291
100. Proteome Sci. 2023. 21(6) doi: 10.1186/s12953-023-00207-8
101. Viruses. 2023. 15. 1491 doi: 10.3390/v15071491
102. Cell Reports. 2023. 42. 113186 doi: 10.1016/j.celrep.2023.113186
103. JBC. 2024. 300(3). 1057044 doi: 10.1016/j.jbc.2024.105704