产品名称
BirA, recombinant, expressed in E. coli, ≥65% (SDS-PAGE)
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
Application
可用于研究酶动力学、抑制剂筛选和选择性分析。
Biochem/physiol Actions
生物素连接酶 BirA 控制 大肠杆菌 的生物素合成。它将生物素送入新陈代谢。作为一种同源二聚体，它负性调控生物素合成操纵子。BirA还可以与乙酰辅酶A羧化酶的生物素受体蛋白一起催化翻译后生物素化。 它可以使人类组蛋白生物素化。
General description
生物素连接酶BirA（GenBank 登记号AP012306 (3602298-3603260)）氨基酸 2-321（末端）具有 His-FLAG-标签，分子量 37.1kDa，表达于大肠杆菌细胞表达系统中。
Physical form
溶于 50mM Tris-HCl，pH 8.0，50mM NaCl，150 mM 咪唑，3mM DTT 和 5％甘油中。
wgk
WGK 1
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
存储类别
6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
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)
Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.
Kobza K, et al.
Bmb Reports, 41, 310-315 (2008)
Yifeng Li et al.
Protein expression and purification, 82(1), 162-167 (2012-01-10)
The extremely tight binding between biotin and avidin or streptavidin makes labeling proteins with biotin a useful tool for many applications. BirA is the Escherichia coli biotin ligase that site-specifically biotinylates a lysine side chain within a 15-amino acid acceptor
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
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