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G8880

Sigma-Aldrich

Glutaminase from Escherichia coli

Grade V, lyophilized powder, 50-200 units/mg protein

Sinónimos:

L-Glutamine amidohydrolase

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About This Item

Número de CAS:
9001-47-2
Comisión internacional de enzimas:
3.5.1.2 (BRENDA, IUBMB)
MDL number:
MFCD00131193
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Escherichia coli

Quality Level

200

type

Grade V

form

lyophilized powder

specific activity

50-200 units/mg protein

mol wt

110 kDa

composition

Protein, ~30% biuret

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.

Unit Definition

One unit will deaminate 1.0 μmole of L-glutamine per min at pH 4.9 at 37 °C.

Physical form

Lyophilized powder containing potassium succinate and EDTA

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
0000193233
0000193234
0000193233
0000193234
0000145909

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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)
Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis
Brown G, et al.
Biochemistry, 47(21), 5724-5735 (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)
Selective flow injection procedures for the determination of nitrogen containing analytes by gasdialytic-fluorimetric detection of enzymatically generated ammonia
Mana H and Spohn U
Analytica Chimica Acta, 325(1-2), 93-104 (1996)
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