Analytical Data
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基因名
OX
- Application
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别名
OX；MOX1；MOX2；；OX-2 membrane glycoProtein
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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
P41217
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表达区间
1-278aa
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氨基酸序列
MERLVIRMPFSHLSTYSLVWVMAAVVLCTAQVQVVTQDEREQLYTPASLKCSLQNAQEALIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNSTITFWNITLEDEGCYMCLFNTFGFGKISGTACLTVYVQPIVSLHYKFSEDHLNITCSATARPAPMVFWKVPRSGIENSTVTLSHPNGTTSVTSILHIKDPKNQVGKEVICQVLHLGTVTDFKQTVNKGYWFSVPLLLSIVSLVILLVLISILLYWKRHRNQDRGELSQGVQKMT
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分子量
31.2 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
OX recombinant proteins are an area of increasing interest in biotechnology and biomedical research, primarily due to their potential applications in therapeutic development and diagnostics. The OX protein family, known for their roles in cell signaling, immune response, and metabolic regulation, has garnered attention for their involvement in various diseases, including cancer and autoimmune disorders. The ability to produce OX proteins through recombinant DNA technology allows for large-scale production and better characterization, facilitating the understanding of their biological functions and mechanisms. In recent years, advancements in cloning, expression systems, and purification techniques have enhanced the feasibility of studying these proteins in vitro and in vivo. Furthermore, the recombinant OX proteins are being explored as candidates for vaccine development and as therapeutic agents due to their specificity and potential for targeted delivery. Research in this field aims to elucidate the structural properties and functional dynamics of OX proteins, profile their interactions with other biomolecules, and assess their efficacy in clinical applications. With ongoing developments in protein engineering and synthetic biology, the study of OX recombinant proteins holds promise for significant contributions to modern medicine and therapeutic innovations.
