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Merck

G6133

Sigma-Aldrich

L-Glutamic acid γ-(p-nitroanilide) hydrochloride

γ-glutamyl transpeptidase substrate

Sinónimos:

L-γ-Glutamyl-p-nitroanilide

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About This Item

Fórmula empírica (notación de Hill):
C11H13N3O5 · HCl
Número de CAS:
Peso molecular:
303.70
Número CE:
Número MDL:
Código UNSPSC:
12352204
ID de la sustancia en PubChem:
NACRES:
NA.83

Nivel de calidad

Análisis

≥98% (HPLC)

formulario

powder

solubilidad

water: 5 mg/mL, clear, yellow

temp. de almacenamiento

2-8°C

cadena SMILES

Cl.NC(CCC(=O)Nc1ccc(cc1)N(=O)=O)C(O)=O

InChI

1S/C11H13N3O5.ClH/c12-9(11(16)17)5-6-10(15)13-7-1-3-8(4-2-7)14(18)19;/h1-4,9H,5-6,12H2,(H,13,15)(H,16,17);1H

Clave InChI

OJEVFSFTVARWQX-UHFFFAOYSA-N

Aplicación

L-Glutamic acid γ-(p-nitroanilide) hydrochloride has been used as a solute carrier family 1 member 5 (SLC1A5) inhibitor:
  • or an inhibitor of the cell membrane glutamine transporter to study the effects of blocking glutamine uptake on esophageal adenocarcinoma (EACC) and thioredoxin-interacting protein (TXNIP)
  • in glutamine ELISA assay to treat confluent differentiated uninfected human colonoid monolayer (HCM) in apical and basolateral compartments to study its effects
  • to study its effect on SLC1A5_var-mediated mitochondrial glutamine transport inhibition
  • to study its effects on cellular glutathione levels, cellular reactive oxygen species (ROS) levels, and mitochondrial ROS levels

Acciones bioquímicas o fisiológicas

L-Glutamyl-p-nitroanilide (GPNA) is commonly used to block the glutamine (Gln) transporter alanine-serine-cysteine transporter 2 (ASCT2). It can also inhibit sodium-dependent and independent amino acid transporters. GPNA, γ-glutamyltransferase (GGT) substrate plays a key role in the hydrolysis of its γ-glutamyl bond and the subsequent release of the chromogen, p-nitroaniline (PNA).

Sustratos

Substrate for γ-glutamyl transpeptidase

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Los clientes también vieron

Paul L Feingold et al.
Molecular cancer therapeutics, 17(9), 2013-2023 (2018-06-24)
In 2017, an estimated 17,000 individuals were diagnosed with esophageal adenocarcinoma (EAC), and less than 20% will survive 5 years. Positron emission tomography avidity is indicative of high glucose utilization and is nearly universal in EAC. TXNIP blocks glucose uptake
Alessandro Corti et al.
Scientific reports, 9(1), 891-891 (2019-01-31)
L-γ-Glutamyl-p-nitroanilide (GPNA) is widely used to inhibit the glutamine (Gln) transporter ASCT2, but recent studies have demonstrated that it is also able to inhibit other sodium-dependent and independent amino acid transporters. Moreover, GPNA is a well known substrate of the
Alessandro Corti et al.
Scientific reports, 9(1), 891-891 (2019-01-31)
L-γ-Glutamyl-p-nitroanilide (GPNA) is widely used to inhibit the glutamine (Gln) transporter ASCT2, but recent studies have demonstrated that it is also able to inhibit other sodium-dependent and independent amino acid transporters. Moreover, GPNA is a well known substrate of the
Long-Liu Lin et al.
Applied microbiology and biotechnology, 73(1), 103-112 (2006-07-20)
A truncated gene from Bacillus lichenifromis ATCC 27811 encoding a recombinant gamma-glutamyltranspeptidase (BLrGGT) was cloned into pQE-30 to generate pQE-BLGGT, and the overexpressed enzyme was purified from the crude extract of IPTG-induced E. coli M15 (pQE-BLGGT) to homogeneity by nickel-chelate
M Moriguchi et al.
Archives of microbiology, 144(1), 15-19 (1986-02-01)
Three gamma-glutamyltranspeptidase (enzymes I, II and III) were partially purified from the cell free extracts of the cultured mycelia of Morchella esculenta Fr. The molecular masses of enzymes were 155,000 (I), 219,000 (II) and 102,000 (III). All of them catalyzed

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