Analytical Data
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Gene name
pla
- Application
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Alternative Names
pla；CLEC13C；Secretory phospholipase A2 receptor
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Species
E.coli
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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
P0A921
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Expression Region
21-289aa
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AA Sequence
QEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF
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Molecular Weight
32.3 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
PLA (Phospholipase A) recombinant proteins have garnered significant interest in recent years due to their diverse biological functions and potential applications in various fields, including medicine, biotechnology, and food science. Phospholipases are enzymes that hydrolyze phospholipids, leading to the release of fatty acids and lysophospholipids, which play crucial roles in cell signaling, membrane dynamics, and inflammatory responses. The recombinant production of PLA proteins allows for a more controlled and efficient study of their biochemical properties and enzymatic activities. Researchers focus on characterizing these enzymes to understand their mechanisms and to explore their therapeutic potential, particularly in treating inflammatory diseases, cancer, and microbial infections. Additionally, PLA recombinant proteins are being investigated for their applications in food emulsification and preservation, where they can enhance texture and stability. The development of advanced expression systems and purification techniques has facilitated the large-scale production of these proteins, making it possible to conduct extensive structural and functional analyses. As the understanding of PLA's roles in health and disease continues to evolve, the research on their recombinant forms holds promise for innovative applications in healthcare and industry.
