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乙酰化赖氨酸抗体

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

简单介绍:乙酰化赖氨酸抗体以乙酰化多肽为免疫原,抗体是经过免疫亲和柱纯化,抗体特异性好、纯度高。能广泛识别各种动植物的乙酰化蛋白,是您研究乙酰化蛋白的好工具。

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详细内容

Acetyl Lysine Antibody


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



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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

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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


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