Analytical Data
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基因名
SELM
- Application
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别名
SELM;SELM;SelenoProtein M
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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
Q8WWX9
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表达区间
24-145aa
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氨基酸序列
ATAYRPDWNRLSGLTRARVETCGGSQLNRLKEVKAFVTQDIPFYHNLVMK HLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQ VPPEYVWAPAKPPEETSDHADL
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分子量
14 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
SELM (Selenoprotein M) is a selenoprotein that plays a crucial role in various biological processes, including antioxidant defense, redox signaling, and modulation of cellular metabolism. Research has shown that SELM is involved in the regulation of selenium homeostasis and has implications in health and disease, particularly in relation to oxidative stress and inflammatory responses. Its unique selenium incorporation at specific cysteine residues allows SELM to exert its functions in protecting cells from oxidative damage. Altered expression of SELM has been linked to various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders. Therefore, understanding the structure-function relationship and the molecular mechanisms underlying SELM’s actions is essential for elucidating its biological significance. Studying SELM in recombinant forms enables researchers to investigate its properties in detail, assess its interactions with other molecular partners, and explore its potential therapeutic applications. Moreover, SELM's role in selenium-dependent pathways highlights the importance of trace elements in human health, making it a focal point of research in nutritional biochemistry and disease prevention. As current findings pave the way for novel therapeutic strategies, the ongoing investigation of SELM continues to provide insights into its multifaceted roles in cellular physiology and its potential as a biomarker or target for therapeutic intervention in selenium-related diseases.












