Analytical Data
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基因名
RPN1
- Application
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别名
RPN1；Dolichyl-diphosphooligosaccharide--Protein glycosyltransferase subunit 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P04843
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表达区间
44-427aa
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氨基酸序列
SHLAKVTAEVVLAHLGGGSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVH
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分子量
70.6kDa
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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
RPN1, a key subunit of the 26S proteasome, plays a crucial role in the ubiquitin-proteasome pathway, which is vital for protein degradation and cellular regulation. This reorganization of proteins is essential for maintaining homeostasis, regulating the cell cycle, and responding to stress. Research into RPN1 has gained momentum due to its implications in various diseases, including cancer and neurodegenerative disorders. Abnormalities in proteasome function, influenced by RPN1, can lead to the accumulation of misfolded proteins, contributing to pathogenesis. Understanding the structure and function of RPN1 is therefore imperative for developing therapeutic strategies aimed at restoring proper proteasomal activity. Recent studies involving the recombinant expression of RPN1 have facilitated in-depth exploration of its mechanisms, interactions, and effects on cellular pathways. These advancements could pave the way for novel interventions in diseases associated with proteasome dysfunction, highlighting the significance of RPN1 in both basic and applied biomedical research.
