Analytical Data
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Gene name
LOR
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23490
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Expression Region
Ser210~Lys312
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Molecular Weight
15kDa
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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
Related Products
Protein Description
LOR (Lipid-Associated Protein) recombinant proteins have garnered significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and vaccine development. These proteins are derived from their natural counterparts, which play crucial roles in cellular processes such as lipid metabolism, membrane integrity, and cell signaling. The recombinant production of LOR proteins allows for enhanced understanding of their structural and functional properties, enabling the exploration of their mechanisms in health and disease. Moreover, advancements in genetic engineering techniques have facilitated the manipulation of LOR sequences, leading to optimized expression systems and improved yields. As a result, researchers are investigating the use of LOR recombinant proteins as therapeutic agents, diagnostic tools, and even as adjuvants in vaccine formulations. These studies are particularly relevant in the context of infectious diseases and metabolic disorders, where precise targeting of LOR-associated pathways may provide innovative treatment strategies. Additionally, the ongoing research emphasizes the need for detailed characterization of these proteins to ensure their safety and efficacy in clinical applications. Overall, the study of LOR recombinant proteins represents a promising frontier in the convergence of molecular biology and therapeutic innovation, aiming to address significant challenges in modern medicine.
