Acetylated-Lysine Mouse mAb (Ac-K-103)

• 产品编号：CST-9681S      品牌：CST       原厂货号：9681S
• 产品分类：抗体 > 一抗 > 蛋白特异性一抗
• 应用分类：

描述：

Acetylated-Lysine Mouse mAb (Ac-K-103)乙酰化赖氨酸的鼠单抗抗识别转录后修饰为赖氨酸残基ε-氨基乙酰化的蛋白质。此抗体可识别不同背景序列中的乙酰化赖氨酸。研究显示它可以识别乙酰化的组蛋白、p53、CBP、PCAF和化学乙酰化的BSA。（美国专利号：6,441,140、6,982,318、7,259,022、7,344,714；U.S.S.N. 11,484,485；及所有国外相应专利）。该单克隆抗体用合成的含乙酰化赖氨酸的肽段库免疫动物制备。赖氨酸的乙酰化如同丝氨酸、苏氨酸和酪氨酸的磷酸化一样，是一种控制蛋白活性的重要可逆手段。四个核心组蛋白（H2A, H2B, H3, H4）的保守氨基末端区域均包含赖氨酸，可以被组蛋白乙酰转移酶（HATs）乙酰化和组蛋白去乙酰酶（HDACs）去乙酰化（1）。组蛋白、转录因子和其它蛋白的乙酰化/去乙酰化信号最终影响多个细胞过程，包括染色体结构、基因活性、细胞生长、分化和凋亡等（2-6）。最近的蛋白组学研究显示赖氨酸残基的乙酰化是蛋白翻译后修饰的广泛而重要的手段，可以影响控制细胞周期、代谢、生存、肌动蛋白聚合和核转运相关的数千种蛋白。蛋白质乙酰化调节障碍在癌症和多聚谷氨酰胺疾病中发现（9），HDACs也成为目前正在开发的有希望的抗癌药物靶点（10）。

1. Hassig, C.A. and Schreiber, S.L. (1997) Curr Opin Chem Biol 1, 300-8.
2. Allfrey, V.G. et al. (1964) Proc Natl Acad Sci USA 51, 786-94.
3. Liu, L. et al. (1999) Mol Cell Biol 19, 1202-9.
4. Boyes, J. et al. (1998) Nature 396, 594-8.
5. Polevoda, B. and Sherman, F. (2002) Genome Biol 3, reviews 0006.
6. Yoshida, M. et al. (2003) Prog Cell Cycle Res 5, 269-78.
7. Kim, S.C. et al. (2006) Mol Cell 23, 607-18.
8. Choudhary, C. et al. (2009) Science 325, 834-40.
9. Hughes, R.E. (2002) Curr Biol 12, R141-3.
10. Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18.

原厂资料：

Specificity / Sensitivity

Acetylated-Lysine Mouse mAb (Ac-K-103) detects proteins only when posttranslationally modified by acetylation on the epsilon-amine groups of lysine residues. Detection of acetylated lysine by this antibody is largely independent of surrounding amino acid sequence. The antibody has been shown to recognize acetylated proteins including histones, p53, CBP, PCAF and chemically acetylated BSA. (U.S. Patent No's.: 6,441,140; 6,982,318; 7,259,022; 7,344,714; U.S.S.N. 11,484,485; and all foreign equivalents.)

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic acetylated lysine-containing peptide.

Background

Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. The conserved amino-terminal domains of the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (1). Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis (2-6). Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of posttranslational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport (7,8). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (9), and HDACs have become promising targets for anti-cancer drugs currently in development (10).

1. Hassig, C.A. and Schreiber, S.L. (1997) Curr Opin Chem Biol 1, 300-8.
2. Allfrey, V.G. et al. (1964) Proc Natl Acad Sci USA 51, 786-94.
3. Liu, L. et al. (1999) Mol Cell Biol 19, 1202-9.
4. Boyes, J. et al. (1998) Nature 396, 594-8.
5. Polevoda, B. and Sherman, F. (2002) Genome Biol 3, reviews 0006.
6. Yoshida, M. et al. (2003) Prog Cell Cycle Res 5, 269-78.
7. Kim, S.C. et al. (2006) Mol Cell 23, 607-18.
8. Choudhary, C. et al. (2009) Science 325, 834-40.
9. Hughes, R.E. (2002) Curr Biol 12, R141-3.
10. Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM
NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not
aliquot the antibody