A. aeolicus BPL/BiolD2 Antibodies

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
ESG020
Anti-A. aeolicus BPL/BiolD2 [SS 3A5-E2] Antibody
100ug 4-6 weeks
Regular Price:$299.00
On Sale:
ESG019
Anti-A. aeolicus BPL/BiolD2 [SS QD1] Antibody
100ug 4-6 weeks
Regular Price:$299.00
On Sale:
Specifications

Product Type: Antibody
Accession ID: O66837, 1193255
Antigen: BPL/BioID2
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

References
  1. 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.
  2. 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.
  3. 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.
  4. Clarke, D. J., J. Coulson, R. Baillie, D. J. Campopiano. 2003. Biotinylation in the hyperthermophile Aquifex aeolicus. Eur J Biochem. 270(6):1277-87.
  5. 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.
  6. 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.

If you publish research with this product, please let us know so we can cite your paper.

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