Analytical Data
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Gene name
LPC
- Application
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Alternative Names
LPC；MFSD2；NLS1；Sodium-dependent lysophosphatidylcholine symporter 1
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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
P04083
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Expression Region
5-346aa
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AA Sequence
SEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
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Molecular Weight
42.3 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
Related Products
Protein Description
LPC (Lysophosphatidylcholine) is a naturally occurring phospholipid that plays a crucial role in various biological processes, including cell signaling, inflammation, and lipid metabolism. Its functions are closely linked to numerous pathological conditions, such as cardiovascular diseases, neurological disorders, and cancers. Research on LPC has expanded significantly due to its potential as a biomarker for disease diagnosis and as a target for therapeutic interventions. The recombinant production of LPC-related proteins has become a focal area in biochemical research, helping to elucidate the mechanisms underlying LPC's biological effects. By utilizing techniques such as recombinant DNA technology, scientists can produce these proteins in a controlled environment, facilitating detailed studies on their structure-function relationships and interactions with other biomolecules. Furthermore, the reconstitution of LPC in various experimental systems allows researchers to explore its role in cellular processes and its impact on health and disease. Consequently, LPC recombinant protein research not only enhances our understanding of fundamental biological mechanisms but also opens avenues for developing targeted therapies that leverage LPC's properties to treat various disorders. The ongoing exploration of LPC and its related proteins is poised to significantly contribute to the fields of biomedicine and pharmaceutical development.
