重组人Rb蛋白(ab59982)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% Densitometry
- Tags: GST tag N-Terminus
- Suitable for: SDS-PAGE
描述
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产品名称
重组人Rb蛋白
参阅全部 Rb 蛋白酶 -
纯度
> 90 % Densitometry. -
表达系统
Escherichia coli -
蛋白长度
Protein fragment -
无动物成分
No -
性质
Recombinant -
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种属
Human -
预测分子量
62 kDa -
氨基酸
46 to 378 -
标签
GST tag N-Terminus
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技术指标
Our Abpromise guarantee covers the use of ab59982 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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应用
SDS-PAGE
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形式
Liquid -
Concentration information loading...
制备和贮存
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稳定性和存储
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.50
Constituents: 0.00174% PMSF, 0.00386% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.788% Tris HCl, 25% Glycerol (glycerin, glycerine), 0.8766% Sodium chloride, 0.30732% Glutathione, 0.00292% EDTA
常规信息
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别名
- Exon 17 tumor GOS561 substitution mutation causes premature stop
- GOS563 exon 17 substitution mutation causes premature stop
- OSRC
see all -
功能
Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity. -
组织特异性
Expressed in the retina. -
疾病相关
Childhood cancer retinoblastoma
Bladder cancer
Osteogenic sarcoma -
序列相似性
Belongs to the retinoblastoma protein (RB) family. -
结构域
The Pocket domain binds to the threonine-phosphorylated domain C, thereby preventing interaction with heterodimeric E2F/DP transcription factor complexes. -
翻译后修饰
Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV E7 and adenovirus E1A bind to the underphosphorylated, active form of pRb. Phosphorylation at Thr-821 and Thr-826 promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-795 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition. Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis.
N-terminus is methylated by METTL11A/NTM1 (By similarity). Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression. Monomethylation at Lys-860 by SMYD2 promotes interaction with L3MBTL1.
Acetylation at Lys-873 and Lys-874 regulates subcellular localization, at least during keratinocytes differentiation. -
细胞定位
Nucleus. - Information by UniProt
实验方案
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
数据表及文件
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SDS download
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Datasheet download
文献 (0)
ab59982 尚未被引用在任何文献中。