Analytical Data
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Gene name
LIPI
- Application
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Alternative Names
PRED5; LPDL; CT17; Membrane-Associated Phospholipase A1 Beta; Cancer/Testis Antigen 17; Membrane-associated phosphatidic acid-selective phospholipase A1-beta
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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
Q6XZB0
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Expression Region
Met1~Phe334
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Molecular Weight
40 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
LIPI, or Lipid-Induced Protein, is a key focus in the field of molecular biology due to its significant role in lipid metabolism and cell signaling. Research surrounding LIPI recombinant proteins has gained momentum in recent years, driven by the growing understanding of how lipid interactions influence various biological processes, including inflammation, insulin signaling, and metabolic disorders. The synthesis of recombinant LIPI proteins has accelerated the exploration of their structure-function relationships, allowing scientists to dissect the mechanisms by which these proteins operate within cellular environments. The ability to produce LIPI in a controlled setting offers a valuable tool for elucidating its biochemical properties and potential therapeutic applications. Furthermore, investigations into LIPI's interactions with other biomolecules could lead to novel strategies for treating diseases linked to lipid dysregulation, such as diabetes and cardiovascular disorders. Overall, the study of LIPI recombinant proteins holds promise for advancing our knowledge of lipid biology and developing innovative medical interventions.
