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| μMACS™ and MultiMACS™ Streptavidin Kits |
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| Magnetic protein isolation via biotinylated capture probes |
µMACS™ and MultiMACS™ Streptavidin Kits take advantage of the well-established MACS® Technology; thus, allowing fast and specific isolation of proteins and their interacting partners by utilizing µMACS Streptavidin MicroBeads and a biotinylated capture probe.
The extremely small, superparamagnetic, and non-sedimenting µMACS MicroBeads are only about 50 nm in diameter and instandly bind to their target, resulting in more captured target proteins per sample. Direct washing of magnetically-labeled proteins in a MACS Column reduces loss of target protein. The renowned in-column technology even facilitates purification of interacting partners and fragile molecular complexes (refer e.g. to fig. 1).
This technology is very useful for the identification and analysis of protein-protein interaction. The principle also works for protein interaction with nucleic acids, such as mRNA, DNA or viral sequences.
Applications of µMACS and MultiMACS Streptavidin Kits:
- Analysis of protein-protein interaction1
- Analysis of DNA-protein interaction2–5
- Analysis of RNA-protein interaction6,7
- Immunoprecipitation with biotinylated antibodies
- Isolation of microRNAs8
- Virus isolation9
- Phage10 and yeast1 display
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| Low- to high-throughput applications |
The µMACS Streptavidin Kit was developed for manual, low-throughput applications with the µMACS Separator.
The procedure can easily be upscaled with the MultiMACS Streptavidin Kits to a semi- or fully-automated, high-throughput processing of up to 96 samples in parallel by utilizing the MultiMACS 96 Separator. |
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| Figure 1 |
| Overview: Specific protein isolation with µMACS Technology. |
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| Figure 2 |
Isolation of specific RNA binding proteins.
A: Yeast extract was incubated with a full-length Mating Factor A2 mRNA bound to a 3'-biotinylated complementary ss-oligo and magnetically labeled with μMACS Streptavidin MicroBeads.
The figure shows the silver-stained SDS gel. Four proteins with apparent molecular weights of 33, 44, 48, and 51 kDa were isolated, which bind specifically to the RNA sequence
B: As a control a magnetically labeled mutant mRNA, missing the binding site for Mating Factor A2 binding proteins was used. The figure shows the silver-stained SDS gel and no specific proteins were isolated. (Courtesy of Dr. Allan Albig, Washington State University, U.S.A.). |
| Figure A |
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| Figure B |
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| Products |
| μMACS Streptavidin Kit |
- for 20 isolations
Components
- 2 mL μMACS Streptavidin MicroBeads
- 4 mL Equilibration Buffer for nucleic acids applications
- 4 mL Equilibration Buffer for protein applications
- 20 μ Columns
Download datasheet
130-074-101
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| μMACS Streptavidin Starting Kit |
- for 20 isolations
Components
- 1 μMACS Streptavidin Kit
- 1 μMACS Separator
- 1 MACS MultiStand
130-091-287
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| MultiMACS Streptavidin Kit (12×8) |
- for 96 isolations
Components
- 5x2 mL Streptavidin MicroBeads
- 5x4 mL Column equilibration buffer for protein applications
- 5x4 mL Column equilibration buffer for nucleic acid applications
- 12 Multi-8 Columns
- 1 MultiColumn Frame
- 1 Deep Well Block (2.5 mL, with sealing foil)
- 1 Microtiter Plate (U-bottom)
130-092-948
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| MultiMACS Streptavidin Kit (4×96) |
- for 384 isolations
Components
- 20x2 mL Streptavidin MicroBeads
- 20x4 mL Column equilibration buffer for protein applications
- 20x4 mL Column equilibration buffer for nucleic acid applications
- 4 Multi-96 Columns with MultiColumn Frames
- 4 Deep Well Blocks (2.5 mL)
- 4 Microtiter Plates (U-bottom)
130-092-949
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| References |
| 1. Feldhaus et al. (2003) Nat. Biotechnol. 21: 163-170. |
| 2. Kalivoda et al. (2003) J. Bacteriol. 185: 4806-4815. |
| 3. Patterson-Fortin, et al. (2006) Nucleic Acids Res.34: 2446–2454. |
| 4. Portis et al. (2003) J. Virol. 77: 105-114. |
| 5. Soe et al. (2003) Nucleic Acids Res. 31: 6585-6592. |
| 6. Albig (2001) MACS&more 5: 6-7. |
| 7. Campalans et al. (2004) Plant Cell 16: 1047–1059. |
| 8. Bentwich et al. (2005) Nature Genetics 37: 766-770. |
| 9. Lupo and Butera (2004) MACS&more 8: 16-17. |
| 10. Siegel et al. (1997) J. Immunol. M. 206: 73-85. |
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