Analytical Data
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Gene name
PLPL
- Application
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Alternative Names
PLPL；Omega-hydroxyceramide transacylase
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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
Q96AD5
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Expression Region
1-504aa
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AA Sequence
MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGA LTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLK VLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPV YCGLIPPSLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSST NIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQGYRDGLRFLQ RNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHL PARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTI RLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELR RVQSLPSVPLSCAAYREALPGWMRNNLSLGDALAKWEECQRQLLLGLFCT NVAFPPEALRMRAPADPAPAPADPASPQHQLAGPAPLLSTPAPEARPVIG ALGL
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Molecular Weight
71 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
The study of PLPL (phospholipase-like protein) recombinant proteins has emerged as a significant area of research due to their potential applications in biotechnology and medicine. Phospholipases are enzymes that play critical roles in various biological processes, including membrane remodeling, signal transduction, and lipid metabolism. PLPLs, a subclass of phospholipases, are particularly intriguing because they exhibit unique substrate specificities and functional properties that can be harnessed for therapeutic purposes. Recent advancements in recombinant DNA technology have facilitated the production of PLPLs in host systems, allowing for detailed functional studies and the development of engineered variants with enhanced catalytic activity or specificity. Researchers are exploring the use of PLPLs in drug delivery systems, therapeutic agents for inflammatory diseases, and as tools for bioremediation. Additionally, understanding the structural and functional dynamics of these enzymes can provide insights into their roles in pathophysiological conditions, potentially leading to the identification of novel biomarkers or targets for disease intervention. The ongoing exploration of PLPL recombinant proteins signifies a promising frontier in enzymology that bridges molecular biology and applied sciences.
