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SRP0417

Sigma-Aldrich

BirA

recombinant, expressed in E. coli, ≥65% (SDS-PAGE)

Sinónimos:

BirA Biotin Ligase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

assay

≥65% (SDS-PAGE)

form

aqueous solution

mol wt

37 kDa

packaging

pkg of 100 μg

NCBI accession no.

AP012306

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.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Storage Class

6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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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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