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The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
GPLD1 is expressed in numerous tissues and cells and specifically cleaves GPI-anchored proteins. Liver has the highest level of GPI-PLD expression and is the primary organ contributing to GPLD1 in the serum. GPLD1 is abundant in serum in which it associates with polipoproteins AI and AIV. Increased serum GPLD1 is associated with insulin resistance and elevated serum triglycerides. Many surface proteins are attached to eukaryotic cell membranes via glycosylphosphatidylinositol (GPI) anchors that are covalently bound to the C-terminus of the protein and cleavage of the GPI moiety by GPLD1, only enzyme known that cleavage GPI anchor, may represent a means of regulating attachment of these proteins to the cell surface, or alternatively, their release into the extracellular environment.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Glycoprotein phospholipase D; Glycosyl-phosphatidylinositol-specific phospholipase D; glycosylphosphatidylinositol phospholipase D; glycosylphosphatidylinositol specific phospholipase D1, isoform 2; GPI-PLD; GPI-specific phospholipase D; MGC22590; Phosphatidylinositol-glycan-specific phospholipase D; PI-G PLD
Gene Aliases: 6330541J12Rik; AW546131; GPIPLD; GPIPLDM; GPLD1; PIGPLD; PIGPLD1; PLD
UniProt ID: (Human) P80108, (Rat) Q8R2H5
Entrez Gene ID: (Human) 2822, (Rat) 291132, (Mouse) 14756
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