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New PhoenixParticle Technology for your Sample preparation

 

A convenient method for immunoprecipitation, protein/peptide purification and cell isolation

Phoenix Pharmaceuticals has successfully applied antibodies onto magnetic particles. Magnetic particles are a convenient affinity support for a variety of assays, which allow easy purification of the target without columns or centrifugation. PhoenixParticles are available pre-coated with Protein A, Protein G, streptavidin, anti-mouse or anti-rabbit antibodies.

Highlights:

         Analysis of plasma or small body fluid samples for MODI-TOF MS. This magnetic-bead-based platform amenable to high-throughput peptide capture and demonstrated that antibody capture followed by mass spectrometry can achieve ion signal enhancements on the order of 103, with precision (CVs <10%) and accuracy.

         Particles respond well to magnetic fields but have no magnetic memory.

         Most separations require a short 2- to 10-minute bench-top procedure.

         Bead specifications surface area: >100 m2/g, 1-2 m or 0.6 1 m diameter depending on application.

         PhoenixParticles are available pre-coated with Streptavidin, Protein A or G, antibodies and can be used for either positive or negative selection .

         Cell can be isolated by binding directly to primary antibody or PhoenixParticles.

         Cell type isolated by PhoenixParticles is determined by the primary antibody bound indirectly to the secondary antibody coated bead.

         Quick and simple method for peptide/protein purification or removal of un-needed proteins/peptides.

References:

1.       Schneider, C., Newman, R.A. et al. (1982). J. Biol. Chem. 257, 10766.

2.       Sisson, T.H. and Castor, C.W. (1990). Immunol. Methods. 127, 215.

3.       Hortin, G. L. (2006). Clin. Chemistry 52, 1223-1237.

4.       Neaey, S.E., et al. (2001). J. Biol. Chem. 276(9), 6645-6655.

5.       Chaudhuri, T.K., et al. (2001). Cell 107, 235-246.

6.       Whiteaker J.R. et al. (2007) Ana. Biochem. (article in press).

 

Figure 1. Human Non-Acylated Ghrelin ( M.W. 3244.71)

Figure 2. Rat Non-Acylated Ghrelin ( M.W. 3188.64 +/- 3)

%PP-005%;%PP-031-31%;PP-031-30%


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