GPT Human, Active

Glutamic-Pyruvate Transaminase Human Recombinant, Active
Cat. No.
BT1288
Source
Escherichia Coli.
Synonyms
Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.
Appearance
Sterile liquid formulation.
Purity

Greater than 95.0% as determined by Analysis by SDS-PAGE.

Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Alanine Aminotransferase Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 495a.a and having a molecular mass of 54,479 Dalton. The amino acid sequence is the same as that of native form of human liver ALT.
The ALT is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Alanine transaminase (ALT) is a transaminase enzyme primarily found in the liver. It plays a crucial role in the metabolism of alanine, an amino acid. ALT catalyzes the reversible transfer of an amino group from alanine to α-ketoglutarate, resulting in the formation of pyruvate and glutamate. ALT levels in serum are clinically measured as a liver function test indicator, providing insights into liver health. Elevated ALT levels may suggest liver damage or disease. Synonyms for ALT include serum glutamate pyruvate transaminase (SGPT) and alanine aminotransferase (ALAT). Clinical measurements are typically expressed in units per liter (U/L).
Description
Recombinant Human Alanine Aminotransferase is produced in E. coli. It is a homodimeric, non-glycosylated polypeptide chain consisting of 495 amino acids with a molecular weight of 54,479 Daltons. The amino acid sequence is identical to that of the native human liver ALT. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile Liquid
Formulation
The protein solution is dialyzed against a buffer containing 40mM sodium acetate (pH 5.5), 1mM DTT, 1mM EDTA, 5mM 2-oxoglutarate, and 0.1mM pyridoxal-5'-phosphate.
Stability
AAT1 is stable at 10°C for 5 days but should be stored below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Greater than 95.0% purity as determined by SDS-PAGE analysis.
Biological Activity
The specific activity is 839 U/mg.
Synonyms
Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.
Source
Escherichia Coli.

Product Science Overview

Structure and Production

The human recombinant form of GPT is produced in E. coli and is a homodimer, non-glycosylated polypeptide chain containing 495 amino acids with a molecular mass of approximately 54,479 Daltons . The amino acid sequence of this recombinant enzyme is identical to that of the native form found in the human liver .

Function and Importance

GPT is involved in cellular nitrogen metabolism and liver gluconeogenesis, starting with precursors transported from skeletal muscles . It is widely used as a biomarker for liver health, as elevated levels of GPT in the serum can indicate liver injury caused by drug toxicity, infection, alcohol, and steatosis .

Clinical Applications

The specific activity of the recombinant GPT enzyme is found to be 1,020 U/mg . It is used in various clinical tests to assess liver function and diagnose liver diseases. The enzyme’s activity levels in the serum are routinely measured to monitor liver health and detect potential liver damage .

Storage and Stability

The recombinant GPT enzyme is stable at 10°C for up to 5 days but should be stored below -18°C to prevent freeze-thaw cycles, which can affect its stability . The enzyme is typically formulated in a sterile liquid solution containing sodium acetate buffer, DTT, EDTA, 2-oxoglutarate, and pyridoxal-5’-phosphate .

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