Analytical Data
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基因名
Rbck1
- Application
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别名
(Heme-oxidized IRP2 ubiquitin ligase 1 homolog)(HOIL-1)(Protein kinase C-binding protein beta-15)(RBCC protein interacting with PKC)(RING-type E3 ubiquitin transferase HOIL-1)(Ubiquitin-conjugating enzyme 7-interacting protein 3)
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种属
Rat
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q62921
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表达区间
1-508aa
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分子量
65.1 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
Rbck1, or RING finger and CHY zinc finger domain-containing protein 1, is a member of the RING-type E3 ubiquitin ligase family, which plays a crucial role in the ubiquitin-proteasome system, a key cellular mechanism for regulating protein degradation and signaling. The enzyme's unique structure allows it to facilitate the transfer of ubiquitin moieties to target proteins, thereby influencing various cellular processes, including cell cycle progression, DNA repair, and immune responses. Recent studies have highlighted Rbck1's involvement in various pathophysiological conditions, such as cancer and neurodegenerative diseases, suggesting that dysregulation of Rbck1 may contribute to aggressive tumor phenotypes and neuronal loss. Researchers are increasingly focused on understanding the specific substrates of Rbck1 and its regulatory mechanisms to uncover its potential as a therapeutic target. The development of recombinant Rbck1 proteins allows for a deeper investigation into its functional roles and interactions within cellular pathways, fostering advancements in targeted therapies. Given the rising significance of ubiquitin ligases in drug development and disease management, studying Rbck1 could provide novel insights into innovative treatments for disease intervention. As a result, creating and characterizing Rbck1 recombinant proteins is a pivotal step toward unraveling its complex biology and therapeutic potential.
