Analytical Data
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基因名
LEI
- Application
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别名
LEI；ELANH2；MNEI；PI2；Leukocyte elastase inhibitor
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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
P30740
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表达区间
1-379aa
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氨基酸序列
MEQLSSANTRFALDLFLALSENNPAGNIFISPFSISSAMAMVFLGTRGNTAAQLSKTFHFNTVEEVHSRFQSLNADINKRGASYILKLANRLYGEKTYNFLPEFLVSTQKTYGADLASVDFQHASEDARKTINQWVKGQTEGKIPELLASGMVDNMTKLVLVNAIYFKGNWKDKFMKEATTNAPFRLNKKDRKTVKMMYQKKKFAYGYIEDLKCRVLELPYQGEELSMVILLPDDIEDESTGLKKIEEQLTLEKLHEWTKPENLDFIEVNVSLPRFKLEESYTLNSDLARLGVQDLFNSSKADLSGMSGARDIFISKIVHKSFVEVNEEGTEAAAATAGIATFCMLMPEENFTADHPFLFFIRHNSSGSILFLGRFSSP
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分子量
58.7kDa
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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
LEI (LEI protein) is a significant focus of research due to its potential roles in various biological processes, including development, cell differentiation, and responses to environmental stimuli. Emerging studies have indicated that LEI proteins are crucial in regulating gene expression and mediating protein interactions within cellular pathways. Understanding the structural and functional properties of LEI proteins can provide insights into their roles in health and disease, particularly in the context of developmental disorders and cancer. Recent advances in proteomics and molecular biology techniques have allowed researchers to dissect the complex mechanisms of LEI proteins at the molecular level, paving the way for novel therapeutic strategies. Researchers are particularly interested in LEI's reorganization, as this process can influence cellular dynamics and functionality. The elucidation of LEI protein structures, interactions, and regulatory mechanisms could lead to a new understanding of the molecular underpinnings of various diseases, highlighting its importance in the field of biomedical research. Overall, the study of LEI proteins stands at the forefront of molecular biology, with the potential to unlock new avenues for targeted therapies and innovative treatments in the future.
