Co-Immunoprecipitation & Protein Binding

Citations:

1. Combined functions of two RRMs in Dead-end1 mimic helicase activity to promote nanos1 translation in the germline.
2. Structural basis of RIP2 activation and signaling
3. Mechanisms of RNA sorting into exosomes

Discover Elusive Interacting Proteins!

MagVigen™ for Co-Immunoprecipitation

• Smaller beads
• Low nonspecific binding
• Higher binding capacity (6x higher)
• Highly biocompatible surfaces
• Less steric hindrance and better accessibility to epitopes
• Optimal surface chemistry
• High throughput automation

Figure 1. Dynamic interactions between Protein A and Protein B were detected by co-immunoprecipitation using MagVigen™ nanobeads. Such interactions were not seen using conventional magnetic beads.

Figure 2. Conventioal magnetic beads may present more steric hindrance and unideal chemistry that to capture elusive molecular/protein interactions/DNA.

Figure 3. Two Lots of MagVigen™ Streptavidin (2mg/mL) and Dynabeads MyOne Streptavidin (10mg/mL) were used to capture 1µg of biotinylated mouse IgG. The amount of uncaptured biotinylated mouse IgG was determined by ELISA. The percentage of captured biotinylated mouse IgG was plotted. MagVigen™ beads showed an antibody binding capacity of 50µg/mg compared to 12µg/mg for Dynabeads.

Figure 4. Capture antibody conjugated MagVigen™ Streptavidin beads (20 µg), Dynabeads MyOne (30 µg) and Merck beads (30 µg) were used in ELISA assay following a standard protocol to detect HBV antigen HBsAg. Bead pellets were reconstituted in 100µl of PBS in the end and 5µl were used to develop color.

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