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ubiquitin specific protease 3 fragment
本产品不向个人销售，仅用作科学研究，不用于任何人体实验及非科研性质的动物实验。
ubiquitin specific protease 3 fragment图片
包装与价格：
包装价格(元)
1mg电议
5mg电议
10mg电议
25mg电议

产品介绍

Deubiquitinates uH2A/uH2B

别名H2N-Ser-Thr-Thr-Ala-Ile-Cys-Ala-Thr-Gly-Leu-OH
Canonical SMILESNC(CO)C(NC(C(O)C)C(NC(C(C)O)C(NC(C)C(NC(C(C)CC)C(NC(CS)C(NC(C)C(NC(C(O)C)C(NCC(NC(CC(C)C)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O
分子式C38H68N10O15S
分子量937.07
溶解度≥ 93.7mg/mL in DMSO
储存条件Store at -20℃
General tipsFor obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.
Shipping ConditionEvaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
产品描述

The ubiquitin specific protease 3 USP3 is a deubiquitinating enzyme for uH2A and uH2B. USP3 dynamically associates with chromatin and deubiquitinates H2A/H2B in vivo. The ZnF-UBP domain of USP3 mediates uH2AUSP3 interaction. Functional ablation of USP3 by RNAi leads to delay of S phase progression and to accumulation of DNA breaks, with ensuing activation of DNA damage checkpoint pathways. In response to ionizing radiation, (1) uH2A redistributes and colocalizes in g-H2AX DNA repair foci and (2) USP3 is required for full deubiquitination of ubiquitin-conjugates/uH2A and g-H2AX dephosphorylation. USP3 is a novel regulator of H2A and H2B ubiquitination, highlight its role in preventing replication stress, and suggest its involvement in the response to DNA double-strand breaks1.
USP3 has been characterized as a functional DUB in vitro, and it is the human DUB most homologous to S. cerevisiae Ubp8, which regulates H2B deubiquitination2-4.

References:
1.F. Nicassio, N. Corrado et al. Human USP3 Is a Chromatin Modifier Required for S Phase Progression and Genome Stability. Current Biology 17, 1972–1977.
2.Sloper-Mould, K.E., Eyre, H.J., Wang, X.W., Sutherland, G.R., and Baker, R.T. (1999). Characterization and chromosomal localization of USP3, a novel human ubiquitin-specific protease. J. Biol. Chem. 274, 26878–26884.
3.Henry, K.W., Wyce, A., Lo, W.S., Duggan, L.J., Emre, N.C., Kao, C.F., Pillus, L., Shilatifard, A., Osley, M.A., and Berger, S.L. (2003). Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Genes Dev. 17, 2648–2663.
4.Zhang, Y. (2003). Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev. 17, 2733–2740.