anti-GPI-PLD, mAb (38A1)

CHF 315.00
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YIF-LF-MA0156100 µlCHF 315.00
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Product Details
Synonyms GPLD1; GPI-PLD; PIGPLD1; PI-G PLD; EC=; Glycoprotein Phospholipase D; GPI-specific Phospholipase D; Phosphatidylinositol-Glycan-Specific Phospholipase D
Product Type Monoclonal Antibody
Clone 38A1
Isotype Mouse IgG1 κ
Immunogen/Antigen Protein purified from human plasma.

Western Blot (1:500)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Mouse IgG1 Isotype Control

Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
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Product Specification Sheet
Datasheet Download PDF

GPI-PLD (glycosylphosphati- dylinositol-specific phospholipase D), a 815-amino acid protein, 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 GPI-PLD in the serum. GPI-PLD is abundant in serum in which it associates with apolipoproteins AI and AIV. Increased serum GPI-PLD 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 GPI-PLD, 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. This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.

Product References

1) Chalasani N et al, J Clin Endocrinol Metab. (2006) vol.91(6): pp.2279-85. (General)
2) MANN KJ et al, Biochem. J. (2004) vol.378: pp.641-8. (General)
3) Gregory P et al, Bone. (2005) vol.37(2): pp.139-47. (General)
4) Raikwar NS et al, Am J Physiol Endocrinol Metab. (2006) vol.290(3): pp.E463-70. (General)

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