Analytical Data
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基因名
USP16
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简介
The USP16 protein is a specific deubiquitinase that targets "Lys-120" of histone H2A (H2AK119Ub), a tag associated with epigenetic transcriptional repression. By catalytically removing this ubiquitin moiety, USP16 acts as a coactivator, promoting subsequent phosphorylation of histone H3 (H3S10ph) 'Ser-11' to achieve mitotic chromosome segregation. USP16 Protein, Human (sf9) is the recombinant human-derived USP16 protein, expressed by sf9 insect cells , with tag free.
- Application
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别名
USP16; Ubiquitin carboxyl-terminal hydrolase 16; Deubiquitinating enzyme 16; Ubiquitin thioesterase 16; Ubiquitin-processing protease UBP-M; Ubiquitin-specific-processing protease 16
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种属
Human
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表达系统
Baculovirus
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y5T5
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表达区间
G2-L823
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蛋白长度
Partial
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
USP16 (Ubiquitin Specific Peptidase 16) is a deubiquitinating enzyme that plays a crucial role in regulating various cellular processes by removing ubiquitin moieties from target proteins, thereby influencing their stability and activity. The study of USP16 has gained significant attention due to its involvement in crucial biological pathways such as cell cycle regulation, DNA damage response, and cellular senescence. Dysregulation of USP16 has been implicated in several diseases, including cancer and age-related disorders, where aberrant protein ubiquitination can lead to the accumulation of damaged proteins or the perpetuation of uncontrolled cellular proliferation. Recent research has highlighted USP16's unique ability to specifically target and deubiquitinate histone proteins, thereby modulating gene expression and impacting chromatin remodeling. As a result, understanding the structure and function of USP16, as well as its regulatory mechanisms, has become a priority in molecular biology and therapeutic research. By exploring the potential of USP16 as a therapeutic target, researchers are investigating small molecules and other inhibitors that could modulate its activity for the treatment of diseases linked to its dysregulation. This body of work aims to elucidate the functional implications of USP16 in both physiological and pathological contexts, paving the way for novel therapeutic strategies that harness the power of deubiquitination in disease intervention.
