Analytical Data
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基因名
sdrD
- Application
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别名
sdrD；CDHF4；Desmoglein-1
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种属
E.coli
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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
O86488
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表达区间
36-330aa
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氨基酸序列
LVGTTLIFGLGNQEAKAAESTNKELNEATTSASDNQSSDKVDMQQLNQEDNTKNDNQKEMVSSQGNETTSNGNKLIEKESVQSTTGNKVEVSTAKSDEQASPKSTNEDLNTKQTISNQEALQPDLQENKSVVNVQPTNEENKKVDAKTESTTLNVKSDAIKSNDETLVDNNSNSNNENNADIILPKSTAPKRLNTRMRIAAVQPSSTEAKNVNDLITSNTTLTVVDADKNNKIVPAQDYLSLKSQITVDDKVKSGDYFTIKYSDTVQVYGLNPEDIKNIGDIKDPNNGETIATAK
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分子量
38.0 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 study of the SDRD (Short Domain Repeat Dipeptide) recombinant protein has emerged as a significant area of research within molecular biology and protein engineering. SDRD proteins are characterized by their unique structural properties and versatile functional potential, which can be leveraged in various biotechnological applications, including drug development, biomaterials, and synthetic biology. The increased interest in SDRD proteins stems from their ability to form distinct conformations, providing insights into protein interactions and stability. Researchers have been focused on elucidating the mechanisms underlying SDRD protein folding and their interactions with other biomolecules. Additionally, advances in genetic engineering techniques have enabled the production of SDRD recombinant proteins in controlled laboratory settings, allowing for in-depth studies of their biochemical properties and functionality. The understanding of SDRD proteins could pave the way for novel therapeutic strategies and innovative solutions to address various biochemical challenges. As the field progresses, ongoing investigations are aimed at optimizing the expression and purification processes of SDRD proteins to enhance their application potential, making it a promising frontier in the realm of protein science.
