Analytical Data
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Gene name
iPLA2
- Application
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Alternative Names
iPLA2；IPLA22；IPLA2G；Calcium-independent phospholipase A2-gamma
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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
Q9NST1
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Expression Region
63-481aa
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AA Sequence
EQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDELLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTLPVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCTPEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKSL
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Molecular Weight
53.7 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
iPLA2 (calcium-independent phospholipase A2) is an enzyme that plays a critical role in phospholipid metabolism, impacting various cellular processes, including membrane remodeling, signal transduction, and inflammatory responses. Its function is particularly significant in the modulation of fatty acid release from membrane phospholipids, which contributes to the production of bioactive lipids involved in cell signaling. Research on iPLA2 has gained momentum due to its implications in various pathophysiological conditions, such as neurodegenerative diseases, cardiovascular disorders, and cancer. Understanding the structure and function of iPLA2 is essential for uncovering its biological roles and therapeutic potential. In recent years, recombinant iPLA2 proteins have been produced for detailed biochemical and structural studies, enabling the exploration of its catalytic mechanisms and substrate specificity. These studies have highlighted the enzyme's importance in lipid metabolism and its potential as a target for drug discovery. The investigation of iPLA2 not only enriches our knowledge of lipid biology but also opens avenues for developing novel therapeutic strategies to modulate its activity in disease contexts.
