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Recombinant Human HDAC1 protein (His tag)

Price: ¥826 ¥476

Size:
100μg 20μg
  • 表达系统: E.coli
  • 蛋白编码: Q13547
别称
GON 10;HD1;HDAC 1;Histone deacetylase 1;RPD3L1
表达系统
E.coli
序列
Arg 9-Asp 321
蛋白编码
Q13547
种属
Human
计算分子量
34.3 kDa
表观分子量
35 kDa
标签
N-His
纯度
> 95 % as determined by reducing SDS-PAGE.
内毒素
Please contact us for more information.
保存条件
Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
运输条件
This product is provided as lyophilized powder which is shipped with ice packs.
制剂
Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
复溶方法
Please refer to the printed manual for detailed information.
背景
Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription. HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes. In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity. Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases. Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents.


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