A. aeolicus BPL/BiolD2 Antibodies
![Anti-A. aeolicus BPL/BiolD2 [SS QD1] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1046_2001202001263210450.jpg "Anti-A. aeolicus BPL/BiolD2 [SS QD1] Antibody")
These mouse IgG1k antibodies were raised against glutathione-S-transferase fused to A. aeolicus biotin protein ligase (BPL) R40G (BioID2) and recognize A. aeolicus BPL/BiolD2.
Highlights:
- Reacts with A. aeolicus BPL/BiolD2
- Suitable for Western Blot, Immunofluorsence and Immunocytochemistry applications
These antibodies were generated to support the recent developments in the BioID, a method that can be used to detect potential interacting proteins. In the BioID method a promiscuous biotin protein ligase (BPL) is fused to a protein of interests and expressed in vivo where it biotinylates proteins in a proximity-dependent manner. The biotinylated proteins can then be affinity purified and identified by mass spectrometry. The original BioID uses a promiscuous BPL from E.coli (BirA R118G), however due to its relatively large size it occasionally hindered proper targeting of the proteins it was fused to. The second generation of the BioID method is based on a BPL from hyperthermophilic bacterium Aquifex aeolicus (A. aeolicusA. aeolicus BPL R40G referred to as BioID2 is the smallest known BPL. The smaller BioID2 not only improved targeting of the bait but also proved to be more efficient in biotinylating proximate proteins.
From a laboratory at Agency for Science, Technology and Research (A*STAR).
These mouse IgG1k antibodies were raised against glutathione-S-transferase fused to A. aeolicus biotin protein ligase (BPL) R40G (BioID2) and recognize A. aeolicus BPL/BiolD2.
Highlights:
- Reacts with A. aeolicus BPL/BiolD2
- Suitable for Western Blot, Immunofluorsence and Immunocytochemistry applications
These antibodies were generated to support the recent developments in the BioID, a method that can be used to detect potential interacting proteins. In the BioID method a promiscuous biotin protein ligase (BPL) is fused to a protein of interests and expressed in vivo where it biotinylates proteins in a proximity-dependent manner. The biotinylated proteins can then be affinity purified and identified by mass spectrometry. The original BioID uses a promiscuous BPL from E.coli (BirA R118G), however due to its relatively large size it occasionally hindered proper targeting of the proteins it was fused to. The second generation of the BioID method is based on a BPL from hyperthermophilic bacterium Aquifex aeolicus (A. aeolicusA. aeolicus BPL R40G referred to as BioID2 is the smallest known BPL. The smaller BioID2 not only improved targeting of the bait but also proved to be more efficient in biotinylating proximate proteins.
From a laboratory at Agency for Science, Technology and Research (A*STAR).
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Antibody |
| Antigen: | BPL/BioID2 |
| Accession ID: | O66837 |
| Molecular Weight: | 27 kDa |
| Isotype: | IgG1k |
| Clonality: | Monoclonal |
| Clone Name: | SS QD1 or SS 3A5-E2 |
| Reactivity: | A. aeolicus |
| Immunogen: | Glutathione-S-transferase fused to A. aeolicus BPL/BioID2 |
| Species Immunized: | Mouse |
| Purification Method: | Protein G |
| Buffer: | PBS, 0.05% (w/v) Sodium Azide |
| Tested Applications: | Western Blot, Immunofluorescence/Immunocytochemistry |
| Storage: | -20C |
| Shipped: | Cold Packs |
- Wilson, K.P., L.M. Shewchuk, R.G Brennan, A.J Otsuka, B.W. Matthews. 1992. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. PNAS. 89(19):9257-61.
- Kim, D. I., S. C. Jensen, K. A Noble, B. Kc, K. H. Roux, K. Motamedchaboki, K. J Roux. 2016. An improved smaller biotin ligase for BioID proximity labeling. Mol Biol Cell. 2016 Feb 24. pii: mbc. E15-12-0844.
- Roux, K. J., D. I. Kim, M. Raida, B. Burke. 2012. A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J Cell Biol. 196(6):801-10.
- Clarke, D. J., J. Coulson, R. Baillie, D. J. Campopiano. 2003. Biotinylation in the hyperthermophile Aquifex aeolicus. Eur J Biochem. 270(6):1277-87.
- Tron C. M., I. W. McNae, M. Nutley, D. J Clarke, A Cooper, M. D. Walkinshaw, R. L. Baxter, D. J. Campopiano. 2009. Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity. J Mol Biol. 387(1):129-46.
- Goodchild, R. E., W. T. Dauer. 2004. Mislocalization to the nuclear envelope: an effect of the dystonia-causing torsinA mutation. PNAS. 101(3):847-52.
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