Glutathione S-transferase (GST, 2.5.1.18) is generally polymerized by two subunits of 25-27kda in the same or different way (the isoelectric point is pH4-5). The N-terminal of its subunit has a conserved serine / tyrosine (Ser / Tyr) residue. Its hydroxyl group forms hydrogen bond with the sulfhydryl group of glutathione (GSH), which is the specific binding site of GSH.

GST is a group of multi-functional isoenzymes widely distributed in various organisms. It is a group of enzymes related to the detoxification function of the liver, mainly in the liver, and trace in the kidney, small intestine, testis, ovary and other tissues. Its main function is to catalyze the sulfhydryl coupling of some endogenous or foreign harmful substances with reduced glutathione and increase its hydrophobicity It is easy to pass through the cell membrane and be discharged from the body after decomposition, so as to achieve the purpose of detoxification. Because the cytoplasm of liver is rich in GST, when the liver cells are damaged, the enzyme is released into the blood rapidly, resulting in the increase of serum GST activity.

GST is often used in the construction of efficient expression vector in gene engineering, so as to co express with some proteins that are difficult to express as molecular chaperones, so as to achieve a soluble expression. In addition, we often use GST antibody to do Western Blot and other experiments to detect whether to achieve gene co expression, so it is of great significance to study it.

[Product Description]

Dosage form: white lyophilized powder or liquid

Preservation buffer: PBS buffer, pH7.0

General information:

Source: gene recombinant expression

Molecular weight: about 26kDa (detected by SDS-PAGE)

Purity: ≥ 90% (SDS-PAGE detection)

Storage conditions: freeze dried powder at 4 ℃ or long-term storage at - 20 ℃

Transportation conditions: ice bag at low temperature

Safety tips: not for human experiment