The K12 strain information can be found on the UniProt website under the following entry: P0A9C5.
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G1270
L-Glutamine Synthetase from Escherichia coli
lyophilized powder, 400-2,000 units/mg protein
Synonym(e):
L-Glutamate:ammonia ligase (ADP-forming)
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100 UNITS
€ 544,00
About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.26
Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
400-2,000 units/mg protein
Aufgereinigt durch
affinity chromatography
Enthält
dithioerythritol as preservative
Zusammensetzung
Protein, ~5% Lowry
Löslichkeit
H2O: soluble 0.95-1.05 mg/mL, clear to hazy
UniProt-Hinterlegungsnummer
Fremdaktivität
ATPase <0.2%
Lagertemp.
−20°C
Angaben zum Gen
Escherichia coli K12 ... glnA(948370)
Allgemeine Beschreibung
L-Glutamine Synthetase from bacteria shows dodecameric structure comprising of 12 active sites. Each active site termed bifunnel, has an ATP and glutamate binding sites. The dodecamer is stabilized by two hexameric rings.[1]
Anwendung
L-Glutamine Synthetase from Escherichia coli has been used in the synthesis of methylglutamine from methylammonium in E coli[2] and in the glutamine synthetase protection activity of human thioredoxin peroxidase enzyme, AOE372.[3]
L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli.[4]
Biochem./physiol. Wirkung
L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine[5]. It is a degradative enzyme for glutamic acid.
Nitrogen starvation dictates the expression of the glutamine synthetase (GS) gene in E. coli.[1] GS plays a key role in ammonia assimilation in bacteria.[6] Adenylylation of GS is catalyzed by adenylyltransferase. Adenylylation of GS modulates its catalytic functionality resulting in glutamine limitation in E coli.[7]
Degradative enzyme for glutamic acid
Einheitendefinition
One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C.
Physikalische Form
Contains potassium phosphate, sodium citrate and magnesium acetate buffer salts
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Kunden haben sich ebenfalls angesehen
Reversible Adenylylation of Glutamine Synthetase Is Dynamically Counterbalanced during Steady-State
Okano H, et al.
Journal of molecular biology, 404(1), 522-536 (2010)
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
Jin DY, et al.
The Journal of Biological Chemistry, 272(49), 30952-30961 (1997)
Kamal Krishna Singh et al.
Plant cell reports, 32(2), 183-193 (2012-10-17)
KEY MESSAGE : The regulation of GS isoforms by WD was organ specific. Two GS isoforms i.e. OsGS1;1 and OsGS2 were differentially regulated in IR-64 (drought-sensitive) and Khitish (drought-tolerant) cultivars of rice. Water deficit (WD) has adverse effect on rice
Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase.
J E Roseman et al.
The Journal of biological chemistry, 262(5), 2101-2110 (1987-02-15)
A soluble Escherichia coli protease has been identified and purified to homogeneity. The protease cleaves glutamine synthetase which has been modified by mixed function oxidation; native glutamine synthetase is not a substrate. Using [14C]glutamine synthetase as a substrate (prepared by
E Rodriguez et al.
Plant physiology and biochemistry : PPB, 62, 19-22 (2012-11-24)
Lead (Pb) is a toxic element, but its putative mutagenic effects in plant cells, using molecular markers, remain to unveil. To evaluate if Pb induces mutagenicity, Pisum sativum L. seedlings were exposed to Pb(2+) (up to 2000 mg L(-1)) for 28 days
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From which E. coli strain is your product G1270 L-Glutamine Synthetase from Escherichia coli isolated?
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