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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.26
MDL number:
form
lyophilized powder
specific activity
100-400 units/mg protein
composition
Protein, ≥30% biuret
solubility
H2O: soluble 0.95-1.05 mg/mL, clear to slightly hazy
UniProt accession no.
storage temp.
−20°C
Gene Information
Escherichia coli K12 ... glnA(948370)
Application
L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli.
Biochem/physiol Actions
Degradative enzyme for glutamic acid
L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine. It is a degradative enzyme for glutamic acid.
Physical form
Lyophilized powder containing buffer salts and stabilizer
Preparation Note
Grown in medium containing glucose and NH4Cl
Other Notes
One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
常规特殊物品
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H S Kingdon et al.
Journal of bacteriology, 94(4), 949-957 (1967-10-01)
The kinetic properties of Escherichia coli glutamine synthetase are markedly influenced by the manner in which the organism is grown. Enzyme obtained from stationary-phase cells grown on glycerol and glutamate is strongely inhibited by each of the eight feedback effectors
Peng Jiang et al.
Biochemistry, 51(45), 9032-9044 (2012-10-24)
Uridylyltransferase/uridylyl-removing enzyme (UTase/UR) catalyzes uridylylation of PII and deuridylylation of PII-UMP, with both activities regulated by glutamine. In a reconstituted UTase/UR-PII cycle containing wild-type UTase/UR, the steady-state modification of PII varied from nearly complete modification to nearly complete demodification as
Alberto Sola-Landa et al.
Nucleic acids research, 41(3), 1767-1782 (2012-12-19)
Interaction of regulatory networks is a subject of great interest in systems biology of bacteria. Phosphate control of metabolism in Streptomyces is mediated by the two-component system PhoR-PhoP. Similarly, the utilization of different nitrogen sources is controlled by the regulator
Jane E Ladner et al.
Biochemistry, 51(51), 10121-10123 (2012-12-14)
The structure of PA5508 from Pseudomonas aeruginosa, a glutamine synthetase (GS) homologue, has been determined at 2.5 Å. Surprisingly, PA5508 forms single hexameric rings rather than the stacked double rings that are characteristic of GS. The C-terminal helical thong motif
Huijuan Jia et al.
Molecular nutrition & food research, 57(2), 291-306 (2012-11-21)
This study addresses the effects of branched-chain amino acids (BCAA) on global gene expression in liver and skeletal muscle and the molecular mechanisms underlying the improvement in liver cirrhosis using DNA microarray analysis combined with RNase protection assay. Male Wistar
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