Acetylated-Lysine (Ac-K²-100) MultiMab? Rabbit mAb mix

• 产品编号：CST-9814S      品牌：CST       原厂货号：9814S
• 产品分类：抗体 > 一抗 > 蛋白特异性一抗
• 应用分类：

描述：

Acetylated-Lysine (Ac-K2-100) Rabbit mAb乙酰化赖氨酸兔单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。研究显示抗体可以与少到0.04ng的化学乙酰化的BSA反应，却不能与非乙酰化的多到25ug的BSA反应。（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乙酰化赖氨酸底物库肽段免疫动物制备。该抗体是两个兔单克隆的混合，以便可以覆盖更大的反应范围。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 (Ac-K2-100) Rabbit mAb detects proteins post-translationally modified by acetylation on the ε-amine groups of lysine residues. The antibody recognizes acetylated lysine in a wide range of sequence contexts. It has been demonstrated to recognize acetylated histones, p53, CBP, PCAF and chemically acetylated BSA. The antibody has been shown to react with as little as 0.04 ng of chemically acetylated BSA while not recognizing up to 25 µg of non-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 acetyl-lysine peptide library. The antibody is formulated from two rabbit monoclones in order to cover broad range of reactivity.

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, 50% glycerol and less than 0.02%
sodium azide. Store at –20°C. Do not aliquot the antibody.