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G8255

Glutamic-Pyruvic Transaminase from porcine heart

lyophilized powder, ≥75 units/mg protein

Synonym(s):

L-Alanine: 2-Oxoglutarate Aminotransferase, Alanine Aminotransferase (catalytic concentration), GPT

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Size/SKUAvailabilityPrice
200 units

Estimated to ship TODAYfromSAINT LOUIS

$153.00
1000 units

Estimated to ship onSeptember 28, 2026fromSAINT LOUIS

$471.00
2000 units

Estimated to ship TODAYfromSAINT LOUIS

$811.00

About This Item

CAS Number:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
232-561-4
MDL number:
Beilstein/REAXYS Number:
3562140
EC Number:
Specific activity:
≥75 units/mg protein
Biological source:
Porcine heart

$153.00


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biological source

Porcine heart

Quality Segment

form

lyophilized powder

specific activity

≥75 units/mg protein

composition

Protein, 75-95%

technique(s)

cell culture | mammalian: suitable

color

light yellow to yellow

foreign activity

L-glutamic dehydrogenase, lactic dehydrogenase and malic dehydrogenase ≤0.01%, glutamic-oxalacetic transaminase ≤0.1%

storage temp.

−20°C

General description

Glutamic-pyruvic transaminase (GPT) is localized majorly in the liver.

Research area: Cell Signaling

Application

Glutamic-Pyruvic Transaminase from porcine heart has been used:
  • in the transamination assay with a racemic mixture of synthetic 3-methyl-2-oxoglutarate
  • to remove glutamate from the cell culture medium used for culturing human embryonic kidney (HEK293) cells
  • in the lactate-dehydrogenase (LD)-coupled alanine transaminase (ALT) reaction kinetic studies

Biochem/physiol Actions

Glutamic-pyruvic transaminase (GPT) mediates the transfer of the amino group to α-ketoglutarate from l-alanine which results in pyruvate and glutamate.Thereby GPT plays a key role in gluconeogenesis and amino acid metabolism. The role of GPT in various kinds of tumors has been reported.
Glutamic-pyruvic transaminase (GPT) is located in most cells in the body, but is found in highest concentrations in the liver. It is used as a marker of liver disease due to the release of GPT into the blood following liver cell necrosis.

Physical form

Lyophilized powder containing citrate and acetate

Preparation Note

Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons

Analysis Note

Protein determined by biuret

Other Notes

One unit will convert 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.6 at 37 °C in the presence of L-alanine.

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G9880G2751SAE0044
description

lyophilized powder, ≥75 units/mg protein

description

ammonium sulfate suspension, ≥75 units/mg protein

description

Type I, ammonium sulfate suspension, 200-500 units/mg protein

description

recombinant, expressed in E. coli ≥12 units/mg protein

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

-

technique(s)

activity assay: suitable

specific activity

≥75 units/mg protein

specific activity

≥75 units/mg protein

specific activity

200-500 units/mg protein

specific activity

≥12 units/mg protein

biological source

Porcine heart

biological source

Porcine heart

biological source

-

biological source

bacterial (arthrobacter sp.)

form

lyophilized powder

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


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Pictograms

Health hazard

Signal Word

Danger

Hazard Codes

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

PPE (personal protective equipment)

Eyeshields, Gloves, type N95 (US)



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Questions

  1. En que se resuspende la GTP para darle estabilidad?

    1 answer
    1. Unfortunately, the solubility and solution stability for this product is not determined. However, various sources state that the enzyme is stable when dissolved in human serum and frozen in aliquots. Please note this has not been validated internally.

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