GDA Human, His
Description
GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
GDA is a member of the ATZ/TRZ family and plays a significant role in microtubule assembly . The enzyme is composed of 454 amino acids and has a molecular mass of approximately 53 kDa . The recombinant form of this enzyme is often produced in Escherichia coli (E. coli) and is tagged with a His-tag at the N-terminus to facilitate purification .
The recombinant human GDA with a His-tag is produced using various expression systems, including E. coli . The His-tag, consisting of a series of histidine residues, allows for easy purification of the protein using nickel affinity chromatography. This method ensures that the protein is obtained in a highly purified form, which is essential for biochemical and structural studies.
Recombinant GDA is used in various research applications, including:
- Enzyme kinetics: Studying the catalytic properties and reaction mechanisms of GDA.
- Structural biology: Determining the three-dimensional structure of GDA to understand its function and interactions with other molecules.
- Drug discovery: Screening for inhibitors or activators of GDA, which could have therapeutic potential for diseases related to purine metabolism.
GDA is an important enzyme for understanding purine metabolism and its associated disorders. Mutations or dysregulation of GDA can lead to various metabolic diseases, making it a target for therapeutic intervention. Additionally, the role of GDA in microtubule assembly suggests its involvement in cellular processes beyond purine metabolism .
In summary, recombinant human GDA with a His-tag is a valuable tool for researchers studying enzyme function, structure, and potential therapeutic applications. Its production in E. coli and purification using nickel affinity chromatography ensure that high-quality protein is available for various scientific investigations.
