Analytical Data
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Gene name
LOR
- Application
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Alternative Names
LOR；LOR；LRN；Loricrin
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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
P23490
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Expression Region
1-316aa
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AA Sequence
MSYQKKQPTPQPPVDCVKTSGGGGGGGGGGGGGCGFFGGGGSGGGSSGSG CGYSGGGGYSGGGCG GGSSGGGGGGGIGGCGGGSGGSVKYSGGGGSSG GGSGCFSSGGGGSGCFSSGGGGSSGGGSGCFS SGGGGSSGGGSGCFSS GGGGFSGQAVQCQSYGGVSSGGSSGGGSGCFSSGGGGGSVCGYSGGGSG GGSGCGGGSSGGSGSGYVSSQQVTQTSCAPQPSYGGGSSGGGGSGGSGC FSSGGGGGSSGCGGGS SGIGSGCIISGGGSVCGGGSSGGGGGGSSVGG SGSGKGVPICHQTQQKQAPTWPSK
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Molecular Weight
61 kDa
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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
LOR (Ligand of Receptor) recombinant proteins have garnered significant attention in molecular biology and biomedicine due to their crucial role in cell signaling and regulation. As key players in various physiological processes, LOR proteins interact with specific receptors, modulating cellular responses and contributing to pathways involved in development, immune response, and disease progression. The ability to produce LOR recombinant proteins in controlled laboratory settings has opened new avenues for research. Scientists aim to understand their structure-function relationships, the mechanisms underlying receptor activation, and the implications of these interactions in health and disease. Advances in recombinant DNA technology allow for the precise engineering of LOR proteins, facilitating the study of their roles in pathological conditions such as cancer, autoimmune disorders, and infectious diseases. Furthermore, LOR proteins hold promise for therapeutic applications, serving as potential targets for drug development or as candidates for novel therapeutic agents. The ongoing research into LOR recombinant proteins is pivotal for uncovering new biological insights and developing innovative strategies for disease intervention.
