Analytical Data
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Gene name
PIGY
- Application
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Alternative Names
PIGY; Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y; Phosphatidylinositol-glycan biosynthesis class Y protein; PIG-Y
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q3MUY2
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Expression Region
1-71 aa
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AA Sequence
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLWTWMGIKLFRHN
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Molecular Weight
34.21 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
PIGY, a member of the PIG family of proteins, plays a critical role in the glycosylphosphatidylinositol (GPI) anchor biosynthesis pathway, which is essential for the proper functioning of numerous cell surface proteins. The GPI anchor is important for cell signaling, adhesion, and immune response, thus underscoring the biological significance of PIGY in various cellular processes. Research into PIGY’s structure and function has gained momentum due to its involvement in various diseases, including certain cancers and genetic disorders associated with defects in GPI anchor biosynthesis. Studies have shown that mutations or aberrant expression of PIGY can lead to altered GPI anchor formation, affecting the localization and activity of critical proteins. Consequently, purifying and characterizing recombinant PIGY protein has become a focal point in understanding its biochemical properties and interactions. Investigating PIGY at the molecular level holds the potential to unravel new therapeutic targets and strategies in treating diseases linked to GPI anchor deficiencies, paving the way for targeted interventions and improved clinical outcomes.
