|Application ||WB, IHC-P, E|
|Calculated MW||92336 Da|
|Antigen Region||679-709 aa|
|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||This GPLD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 679-709 amino acids from the C-terminal region of human GPLD1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GPLD1 Antibody (C-term) is for research use only and 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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