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G8880

Sigma-Aldrich

Glutaminase from Escherichia coli

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

Synonym(s):

L-Glutamine amidohydrolase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Escherichia coli

Quality Level

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 Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Porta-caval shunting changes neuronal sensitivity to ammonia
Raabe W and Onstad G
Journal of the Neurological Sciences, 71(2-3), 307-314 (1985)
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)

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