Invitrogen™ Dynabeads™ Protein G for Immunoprecipitation 

Description

Dynabeads Protein G beads are uniform, 2.8-μm superparamagnetic beads with recombinant Protein G (∼17 kDa) covalently coupled to the surface. Dynabeads Protein G beads provide a great alternative to Sepharose resin or agarose resin for immunoprecipitation (IP) combined with your own antibody, and both manual and automated protocols are available.

Benefits of Dynabeads Protein G beads include:
• Fast and easy—IP in less than 40 minutes with no columns, centrifugations, or time-consuming pre-clearing required
• High performance—high target protein yield with low antibody consumption
• Low background—very low non-specific binding with a high signal-to-noise ratio
• High reproducibility—uniform beads ensure the most consistent results
• Automation ready—automation protocols available with the KingFisher Sample Purification instruments

Gentle separation causes minimal physical stress to proteins
The magnetic separation technology utilized by Dynabeads Protein G is rapid and gentle, causing minimal physical stress to target proteins. This permits the isolation and concentration of labile composites that might otherwise dissociate or be damaged by proteases during long incubation times. Native protein conformation and large protein complexes are preserved.

Binding strength and antibody binding capacity
Dynabeads Protein G beads allow for the isolation of most mammalian immunoglobulins (Ig). The amount of Ig captured depends on the concentration of Ig in the starting sample and on the type and source of the Ig. 100 μL of Dynabeads Protein G will isolate approximately 25–30 μg human IgG from a sample containing 20–200 μg IgG/mL. Predominantly Fc-binding allows optimal Ig orientation.

Dynabeads magnetic beads are not porous in nature such as Sepharose or agarose resins. This means that all antibodies bind to the smooth outer surface of the beads and thus are available to bind the target protein. This translates to a low antibody consumption while obtaining a high yield of the target protein. The smooth bead surface is also responsible for the low non-specific binding that Dynabeads magnetic beads are known for.

Dynabeads immunoprecipitation protocol is fast and easy
The manual IP protocol is simple and can be performed in less than 40 minutes with 3 easy bind-incubate-elute steps. The procedure does not require any pre-clearing due to the low non-specific binding and uses very little antibody while still obtaining a high IP yield, thus saving both time and cost per IP.

The antibody-coated beads can be used in a variety of IP applications such as Co-IP, chromatin IP (ChIP/ChIP sequencing), RNA IP (RIP, RIP sequencing), small-scale IgG purification, and protein purification. The isolated pure target protein can be used in downstream western blot, mass spectrometry analysis, sequencing, etc.

Automation-ready for use with KingFisher purification systems
The 2.8-μm magnetic beads are ideal for high-throughput enrichment. This process can be automated using any of our KingFisher sample purification systems or liquid handlers.

Commercial supply
Our manufacturing sites are ISO 13485-certified. Bead characteristics and manufacturing conditions help ensure consistency and batch reproducibility making them the ideal choice for commercial supply. If you are in the process of customizing Dynabeads Protein G beads in a commercial product or service or need a larger bulk volume of this product, please contact us at oemdynal@lifetech.com or see our Dynabeads OEM page.

Learn more about Dynabeads magnetic beads and KingFisher Sample Purification Systems:
• Dynabeads Protein G beads are also available as a 'ready-to-go' kit with buffers included (Cat. No. 10007D)
• See our immunoprecipitation selection table, data, and references
• Dynabeads magnetic beads selection guide
• See magnets for Dynabeads magnetic beads separations
• KingFisher automation protocols
• Watch a video about the KingFisher Flex instrument

*Sepharose is a trademark of GE Healthcare Bio-Sciences AB.

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