BirA Antibodies
![Anti-BirA [5B11c3-3] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1046_2001202001263210450.jpg "Anti-BirA [5B11c3-3] Antibody")
These mouse IgG1k monoclonal antibodies were raised against glutathione-S-transferase fused to E.coli biotin ligase (BirA) R118G and recognize E. coli BirA.
- Reacts with E. coli BirA
- Clone 5B11c3-3: Binds to amino acids residues 151-321
- Clone 6C4c7: Binds to amino acids residues 2-150 R118G
- Suitable for Western Blot, Immunofluorsence and Immunocytochemistry applications
E.coli BirA is a well-characterized multifunctional protein that either catalyses the transfer of biotin to biotin carboxyl carrier protein (BCCP), a acetyl-CoA carboxylase subunit or, alternatively, binds to the biotin operator resulting in transcriptional repression of the biotin operon. A mutant BirA (R118G) shows loss of DNA binding ability and promiscuity of substrate biotinylation. These properties of BirA R118G were used to develop an in vivo proximity labelling technique that identifies potential interacting proteins (BioID). In the BioID method, a protein of interest is tagged with BirA R118G and expressed in live cells. Addition of the biotin to the culture medium results in biotinylation of proteins in vicinity of the bait. The biotinylated proteins can then be affinity purified with biotin binding proteins such as strepavidin or avidin even under harsh denaturing conditions and subsequently identified by mass spectrometry or immunoblot analysis.
From a laboratory at Agency for Science, Technology and Research (A*STAR).
These mouse IgG1k monoclonal antibodies were raised against glutathione-S-transferase fused to E.coli biotin ligase (BirA) R118G and recognize E. coli BirA.
- Reacts with E. coli BirA
- Clone 5B11c3-3: Binds to amino acids residues 151-321
- Clone 6C4c7: Binds to amino acids residues 2-150 R118G
- Suitable for Western Blot, Immunofluorsence and Immunocytochemistry applications
E.coli BirA is a well-characterized multifunctional protein that either catalyses the transfer of biotin to biotin carboxyl carrier protein (BCCP), a acetyl-CoA carboxylase subunit or, alternatively, binds to the biotin operator resulting in transcriptional repression of the biotin operon. A mutant BirA (R118G) shows loss of DNA binding ability and promiscuity of substrate biotinylation. These properties of BirA R118G were used to develop an in vivo proximity labelling technique that identifies potential interacting proteins (BioID). In the BioID method, a protein of interest is tagged with BirA R118G and expressed in live cells. Addition of the biotin to the culture medium results in biotinylation of proteins in vicinity of the bait. The biotinylated proteins can then be affinity purified with biotin binding proteins such as strepavidin or avidin even under harsh denaturing conditions and subsequently identified by mass spectrometry or immunoblot analysis.
From a laboratory at Agency for Science, Technology and Research (A*STAR).
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Antibody |
| Antigen: | BirA |
| Accession ID: | P06709 |
| Molecular Weight: | 35 kDa |
| Isotype: | IgG1k |
| Clonality: | Monoclonal |
| Clone Name: | 5B11c3-3 or 6C4c7 |
| Reactivity: | E. coli |
| Immunogen: | Glutathione-S-transferase fused to E.coli BirA R118G |
| Species Immunized: | Mouse |
| Epitope: |
Clone 5B11c3-3: Amino acids residues 151-321 of E.coli BirA Clone 6C4c7: Amino acids residues 2-150 R118G of E.coli BirA |
| Purification Method: | Protein G |
| Buffer: | PBS, 0.05% (w/v) Sodium Azide |
| Tested Applications: | Western Blot, Immunofluorescence |
| Storage: | -20C |
| Shipped: | Cold Packs |
- Streaker, E.D., D. Beckett. 2003. Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding. J Mol Biol. 325(5):937-48.
- Kwon, K., E.D. Streaker, S. Ruparelia, D. Beckett. 2000. Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor. J Mol Biol. 304(5):821-33.
- Choi-Rhee, E., H. Schulman, J.E. Cronan. 2004. Promiscuous protein biotinylation by Escherichia coli biotin protein ligase. Protein Sci. 13(11):3043-50.
- 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.
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