Analytical Data
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基因名
ssuE
- Application
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别名
ssuE;ycbP;FMN reductase (NADPH)
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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
P80644
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表达区间
1-191aa
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氨基酸序列
MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGKVVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHRPQFTPNLQTRLDTALETFWQALHRRDVQVPDLLSLRGNAHA
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分子量
26.9 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
The research on ssuE recombinant proteins is rooted in the growing interest in understanding the biochemical and physiological roles of sulfur metabolism in various organisms. The ssuE gene is part of the sulfur assimilation pathway, which is crucial for organisms to incorporate sulfur into essential biomolecules like amino acids and coenzymes. Studies have shown that ssuE encodes a protein involved in the conversion of sulfite to sulfide, a key step in this pathway. Investigating the recombinant form of ssuE provides insights into its enzymatic mechanisms, substrate specificity, and potential regulatory roles within the sulfur metabolism framework. Moreover, utilizing recombinant DNA technology allows for the expression and purification of the ssuE protein, facilitating detailed structural and functional analyses. This research not only enhances our understanding of microbial ecology and the sulfur cycle but also has implications for biotechnological applications, such as bioenergy production and bioremediation, where sulfur assimilation plays a vital role. By elucidating the properties and functions of ssuE recombinant proteins, scientists aim to develop novel strategies to manipulate sulfur metabolic pathways, potentially leading to advancements in environmental biotechnology and agricultural practices. Overall, the study of ssuE recombinant proteins represents a significant contribution to our comprehension of sulfur dynamics and its broader impacts on ecosystem health and sustainability.












