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BD Transduction Laboratories™ Purified Mouse Anti-GPI-Phospholipase D
クローン 15/GPI-Phospholipase D
(RUO)




Western blot analysis of GPI-Phospholipase D on human plasma lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-GPI-Phospholipase D.

Immunofluorescent staining of WI-38 cells.


BD Transduction Laboratories™ Purified Mouse Anti-GPI-Phospholipase D

BD Transduction Laboratories™ Purified Mouse Anti-GPI-Phospholipase D

Regulatory Statusの凡例
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation and Storage
推奨アッセイ手順
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Glycosylphosphatidylinositol (GPI)-anchored proteins are involved in the regulation of numerous cell-surface activities including the complement cascade, activation of plasminogen, T-cell activation, cell-to-cell adhesion, and macromolecule transport through the membrane. GPI-containing proteins are very abundant at the caveolae. GPI-specific phospholipase D (GPI-PLD) hydrolyzes the covalently bound GPI moiety which functions as an anchor for many cell-surface proteins. Present at high levels in the plasma, GPI-PLD is also secreted by some cell types in culture. This protein releases the GPI-anchored, complement regulatory protein decay accelerating factor (DAF) from HeLa cells, as well as the basic fibroblast growth factor (bFGF)-bound heparin sulfate proteoglycan from bone marrow stromal cells. GPI-PLD contains Ca2+ and Zn2+ binding sites and bears some further structural and perhaps functional similarities to the integrins.
Development References (4)
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Huang KS, Li S, Fung WJ. Purification and characterization of glycosyl-phosphatidylinositol-specific phospholipase D. J Biol Chem. 1990; 15(29):17738-17745. (Biology). View Reference
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Li JY, Hollfelder K, Huang KS, Low MG. Structural features of GPI-specific phospholipase D revealed by proteolytic fragmentation and Ca2+ binding studies. J Biol Chem. 1994; 269(46):28963-28971. (Biology). View Reference
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Metz CN, Brunner G, Choi-Muira NH. Release of GPI-anchored membrane proteins by a cell-associated GPI-specific phospholipase D. EMBO J. 1994; 13(7):1741-1751. (Biology). View Reference
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Metz CN, Zhang YY, Guo Y. Production of the glycosylphosphatidylinositol-specific phospholipase D by the islets of Langerhans. J Biol Chem. 1991; 266(27):17733-17736. (Biology). View Reference
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
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