Analytical Data
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基因名
OTUD5
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简介
The OTUD5 protein is a deubiquitinating enzyme that crucially eliminates the innate immune response through peptidase activity on "Lys-48" and "Lys-63" linked polyubiquitin chains, thereby inhibiting TRAF3-mediated Type I interferon production. It acts as a regulator of neuroectodermal differentiation by cleaving “Lys-48” linked ubiquitin chains to prevent the degradation of chromatin regulators such as ARID1A, HDAC2 and HCF1. OTUD5 Protein, Human (His, FLAG) is the recombinant human-derived OTUD5 protein, expressed by E. coli , with N-6*His, N-Flag labeled tag.
- Application
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别名
OTUD5; OTU domain-containing protein 5; Deubiquitinating enzyme A; DUBA
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种属
Human
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表达系统
E. coli
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标签
N-His;C-Flag
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96G74
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表达区间
G172-G351
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蛋白长度
Partial
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分子量
23.9 KDa
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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
OTUD5, a member of the ovarian tumor domain-containing protein family, has garnered attention in recent years due to its role in regulating protein ubiquitination, a crucial post-translational modification involved in various cellular processes including protein degradation, signal transduction, and cellular responses to stress. Research has shown that OTUD5 functions as a deubiquitinase, specifically removing ubiquitin chains from target proteins, which can influence various signaling pathways. Dysregulation of ubiquitination has been implicated in numerous diseases, including cancer and neurodegenerative disorders, making OTUD5 a potential target for therapeutic intervention. Recent studies have suggested that OTUD5 may contribute to tumor development and progression, highlighting its significance in cancer biology. Additionally, understanding the molecular mechanisms by which OTUD5 interacts with its substrates could provide insights into its functional roles in cellular homeostasis and disease. Consequently, the recombinant expression of OTUD5 and the subsequent analysis of its activity and interactions are essential for elucidating its physiological functions and potential implications in disease mechanisms. This research not only enhances our understanding of the ubiquitin-proteasome system but also opens avenues for developing novel therapeutic strategies aimed at modulating OTUD5's activity in pathological conditions.
