Analytical Data
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Gene name
PLA1
- Application
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Alternative Names
PLA1；NMD；PSPLA1；Phospholipase A1 member A
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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
Q53H76
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Expression Region
26-456aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSDAPPTPQ PKCADFQSAN LFEGTDLKVQ FLLFVPSNPS CGQLVEGSSD LQNSGFNATL GTKLIIHGFR VLGTKPSWID TFIRTLLRAT NANVIAVDWI YGSTGVYFSA VKNVIKLSLE ISLFLNKLLV LGVSESSIHI IGVSLGAHVG GMVGQLFGGQ LGQITGLDPA GPEYTRASVE ERLDAGDALF VEAIHTDTDN LGIRIPVGHV DYFVNGGQDQ PGCPTFFYAG YSYLICDHMR AVHLYISALE NSCPLMAFPC ASYKAFLAGR CLDCFNPFLL SCPRIGLVEQ GGVKIEPLPK EVKVYLLTTS SAPYCMHHSL VEFHLKELRN KDTNIEVTFL SSNITSSSKI TIPKQQRYGK GIIAHATPQC QINQVKFKFQ SSNRVWKKDR TTIIGKFCTA LLPVNDREKM VCLPEPVNLQ ASVTVSCDLK IACV
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Molecular Weight
50 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
PLA1 (Phospholipase A1) is a pivotal enzyme involved in the hydrolysis of phospholipids, playing a critical role in various biological processes, including membrane remodeling, signaling pathways, and lipid metabolism. The study of PLA1 recombinant proteins has gained prominence due to their potential applications in biotechnology and medicine. As researchers seek to understand the structure-function relationships of PLA1, recombinant expression systems, such as E. coli or yeast, have been developed to produce these proteins in large quantities. This not only facilitates detailed biochemical characterizations but also enables the exploration of PLA1's roles in pathophysiological conditions, such as inflammation, cancer, and cardiovascular diseases. Furthermore, due to their specific lipid-modifying properties, PLA1 recombinant proteins are being investigated for engineering new therapeutics and developing diagnostic tools. Advances in molecular biology and protein engineering techniques are enhancing our ability to create optimized PLA1 variants with improved stability and activity. Overall, the research surrounding PLA1 recombinant proteins is poised to contribute significantly to our understanding of lipid biology and the development of innovative biomedical applications.
