|Other Names||Phosphatidylinositol-glycan-specific phospholipase D, PI-G PLD, Glycoprotein phospholipase D, Glycosyl-phosphatidylinositol-specific phospholipase D, GPI-PLD, GPI-specific phospholipase D, GPLD1, PIGPLD1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2461b was selected from the C-term region of human GPLD1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Tsang, T.C., et al., FASEB J. 6, A1922-A1922 (1992).
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