Analytical Data
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Gene name
PCYT2
- Application
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Alternative Names
PCYT2;Ethanolamine-phosphate cytidylyltransferase
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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
Q99447
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Expression Region
1-389aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MIRNGRGAAG GAEQPGPGGR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKYNCDFC VHGNDITLTV DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKC PGGRNPWTGV SQFLQTSQKI IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVHRLA ERPYIIAGLH FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY AVTAELLSHF KVDLVCHGKT EIIPDRDGSD PYQEPKRRGI FRQIDSGSNL TTDLIVQRII TNRLEYEARN QKKEAKELAF LEAARQQAAQ PLGERDGDF
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Molecular Weight
46 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
PCYT2, or phosphatidylserine synthase 2, is a crucial enzyme involved in the biosynthesis of phosphatidylserine, a key phospholipid in cellular membranes. It plays a significant role in cellular signaling, apoptosis, and membrane dynamics. The dysfunction of PCYT2 has been linked to various diseases, including neurodegenerative disorders and cancer, making it an important target for therapeutic interventions. The recombinant expression of PCYT2 enables researchers to study its structure-function relationships and regulatory mechanisms in detail. By utilizing recombinant protein techniques, PCYT2 can be produced in a controlled environment, allowing for high-purity protein that is essential for kinetic assays, crystallography, and other biochemical analyses. Understanding the activity and regulation of PCYT2 not only provides insights into lipid metabolism and signaling pathways but also holds potential for the development of targeted therapies aimed at modulating its function in disease contexts. Researchers are particularly interested in how post-translational modifications and interaction with other proteins can influence PCYT2's activity, offering perspectives on novel regulatory mechanisms within lipid biosynthesis. Enhancing our comprehension of PCYT2 could pave the way for innovative strategies to combat diseases driven by lipid imbalances, emphasizing the importance of this enzyme in both health and disease.
