SRP0417
BirA
recombinant, expressed in E. coli, ≥65% (SDS-PAGE)
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UNSPSC Code:
12352200
NACRES:
NA.32
Recommended Products
recombinant
expressed in E. coli
Assay
≥65% (SDS-PAGE)
form
aqueous solution
mol wt
37 kDa
packaging
pkg of 100 μg
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
General description
Biotin ligase BirA (GenBank Accession No. AP012306 (3602298-3603260)) amino acids 2 – 321 (end) with His-FLAG-tag, MW = 37.1 kDa, expressed in an Escherichia coli cell expression system.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
Biotin ligase BirA controls biotin synthesis in Escherichia coli. It sends biotin to metabolism. As a homodimer, it negatively controls the biotin synthetic operon. BirA also catalyzes post-translational biotinylation, by associating with biotin acceptor protein of acetyl-coenzyme A carboxylase. It can biotinylate human histones.
Physical form
Formulated in 50 mM Tris-HCl, pH 8.0, 50 mM NaCl, 150 mM imidazole, 3 mM DTT, and 5% Glycerol.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
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Vandana Chakravartty et al.
Journal of bacteriology, 194(5), 1113-1126 (2012-01-03)
Transcription of the Escherichia coli biotin (bio) operon is directly regulated by the biotin protein ligase BirA, the enzyme that covalently attaches biotin to its cognate acceptor proteins. Binding of BirA to the bio operator requires dimerization of the protein
Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.
Kobza K, et al.
Bmb Reports, 41, 310-315 (2008)
Functional versatility of a single protein surface in two protein:protein interactions.
Adikaram PR and Beckett D
Journal of Molecular Biology, 419, 223-233 (2012)
Hema Chandra Kotamarthi et al.
Cell reports, 30(8), 2644-2654 (2020-02-27)
ATP-powered unfoldases containing D1 and D2 AAA+ rings play important roles in protein homeostasis, but uncertainty about the function of each ring remains. Here we use single-molecule optical tweezers to assay mechanical unfolding and translocation by a variant of the
Bin Yang et al.
Nature communications, 6, 6592-6592 (2015-03-21)
Enterohemorrhagic Escherichia coli (EHEC) is an important foodborne pathogen that infects humans by colonizing the large intestine. Here we identify a virulence-regulating pathway in which the biotin protein ligase BirA signals to the global regulator Fur, which in turn activates
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