G8880
Glutaminase from Escherichia coli
Grade V, lyophilized powder, ≥50 units/mg protein
Synonym(s):
L-Glutamine amidohydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥50 units/mg protein
Biological source:
Escherichia coli
biological source
Escherichia coli
type
Grade V
form
lyophilized powder
mol wt
110 kDa
composition
Protein, ~30% biuret
Quality Level
specific activity
≥50 units/mg protein
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
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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 catalyzes the conversion of glutamine to glutamate.
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.
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.
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
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Porta-caval shunting changes neuronal sensitivity to ammonia
Raabe W and Onstad G
Journal of the Neurological Sciences, 71(2-3), 307-314 (1985)
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
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)
Modulation of metastatic potential of B16F10 melanoma cells by acivicin: synergistic action of glutaminase and potentiation of cisplatin cytotoxicity
Roy S and Maity P
Asian Pacific Journal of Cancer Prevention, 8(2), 301-301 (2007)
Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis
Brown G, et al.
Biochemistry, 47(21), 5724-5735 (2008)
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