Analytical Data
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基因名
GP25L2
- Application
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别名
GP25L2;GP25L2;Transmembrane emp24 domain-containing Protein 9
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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
Q9BVK6
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表达区间
40-197aa
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氨基酸序列
FHIGETEKKCFIEEIPDETMVIGNYRTQLYDKQREEYQPATPGLGMFVEVKDPEDKVILARQYGSEGRFTFTSHTPGEHQICLHSNSTKFSLFAGGMLRVHLDIQVGEHANDYAEIAAKDKLSELQLRVRQLVEQVEQIQKEQNYQRWREERFRQTSE
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分子量
45.5 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
Related Products
Protein Description
The GP25L2 recombinant protein has garnered significant interest in the field of virology and biomolecular research due to its potential implications in understanding viral pathogenesis and developing therapeutic strategies. Originating from certain viral strains, GP25L2 has been studied for its role in modulating immune responses during virus-host interactions. This protein is believed to influence the host's immune evasion tactics, making it a critical target for vaccines and antiviral therapies. Additionally, the study of GP25L2 contributes to the broader understanding of protein interactions and functionalities in viral life cycles. Researchers are exploring the structural and functional properties of GP25L2 through techniques such as X-ray crystallography and biophysical assays to elucidate its mechanisms of action. Insights gained from these investigations are expected to enable the development of targeted interventions that could inhibit viral replication and enhance host defenses. The ongoing exploration of GP25L2 thus represents a vital avenue for advancing our knowledge of viral diseases and improving public health responses.












