G8880
Glutaminase from Escherichia coli
Grade V, lyophilized powder, ≥50 units/mg protein
Synonyme(s) :
L-Glutamine amidohydrolase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥50 units/mg protein
Biological source:
Escherichia coli
Service technique
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Escherichia coli
Quality Level
type
Grade V
form
lyophilized powder
specific activity
≥50 units/mg protein
mol wt
110 kDa
composition
Protein, ~30% biuret
solubility
water: 1 mg/mL (Clear w/Particle to Sl. Hazy w/Particles)
cation traces
NH4+: <0.1 μg/unit
foreign activity
NADH Oxidase ≤0.01%
storage temp.
−20°C
General description
Glutaminase is an amidohydrolase. It has the catalytic domain in the N-terminal and the C-terminal extension possesses STAS domain.
Application
Glutaminase from E.coli has been used:
- for the determination of glutamine from the cerebral cortex tissue extract
- for immobilization on aminopropylsilylated controlled pore glass (CPG) for determination of glutamine
- in combination with acivicin in in vitro melanoma cells and MCF-7 and OAW-42 cells for cell proliferation and invasiveness assay.
Biochem/physiol Actions
Glutaminase from Escherichia coli along with acivicin, a glutamine analog regulates proliferation and invasiveness of cancer cells. Bacterial glutaminase is implicated in increasing the life span of cancer patients by lowering the tumor burden.
Glutaminase catalyzes the conversion of glutamine to glutamate.
Physical form
Lyophilized powder containing potassium succinate and EDTA
Other Notes
One unit will deaminate 1.0 μmole of L-glutamine per min at pH 4.9 at 37 °C.
Classe de stockage
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Contenu apparenté
Acivicin with glutaminase regulates proliferation and invasion of human MCF-7 and OAW-42 cells-An in vitro study
Roy S, et al.
Indian Journal of Experimental Biology, 46, 22-26 (2008)
Ayşegül Erdem et al.
Nature communications, 13(1), 2013-2013 (2022-04-21)
Metabolic programs can differ substantially across genetically distinct subtypes of acute myeloid leukemia (AML). These programs are not static entities but can change swiftly as a consequence of extracellular changes or in response to pathway-inhibiting drugs. Here, we uncover that
Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis
Brown G, et al.
Biochemistry, 47(21), 5724-5735 (2008)