Analytical Data
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Gene name
LEI
- Application
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Alternative Names
LEI；ELANH2；MNEI；PI2；Leukocyte elastase inhibitor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30740
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Expression Region
1-379aa
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AA Sequence
MEQLSSANTRFALDLFLALSENNPAGNIFISPFSISSAMAMVFLGTRGNTAAQLSKTFHFNTVEEVHSRFQSLNADINKRGASYILKLANRLYGEKTYNFLPEFLVSTQKTYGADLASVDFQHASEDARKTINQWVKGQTEGKIPELLASGMVDNMTKLVLVNAIYFKGNWKDKFMKEATTNAPFRLNKKDRKTVKMMYQKKKFAYGYIEDLKCRVLELPYQGEELSMVILLPDDIEDESTGLKKIEEQLTLEKLHEWTKPENLDFIEVNVSLPRFKLEESYTLNSDLARLGVQDLFNSSKADLSGMSGARDIFISKIVHKSFVEVNEEGTEAAAATAGIATFCMLMPEENFTADHPFLFFIRHNSSGSILFLGRFSSP
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Molecular Weight
58.7kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
