NDUFS6 Human
Description
Product Specs
Product Science Overview
Histidine NADH Dehydrogenase Fe-S Protein 6, also known as NDUFS6, is a subunit of Complex I. Complex I plays a crucial role in cellular respiration, facilitating the transfer of electrons from NADH to ubiquinone. This process is essential for the generation of ATP, the primary energy currency of the cell.
NDUFS6 is an iron-sulfur (Fe-S) protein, which means it contains iron-sulfur clusters that are vital for its function. These clusters facilitate the transfer of electrons within the protein complex. The human recombinant form of NDUFS6 is produced using recombinant DNA technology, which allows for the expression of the protein in a host organism, typically E. coli, for research and therapeutic purposes.
The preparation of human recombinant NDUFS6 involves several steps:
- Gene Cloning: The gene encoding NDUFS6 is cloned into an expression vector.
- Transformation: The vector is introduced into a host organism, such as E. coli.
- Expression: The host organism is cultured under conditions that induce the expression of the recombinant protein.
- Purification: The protein is purified using techniques such as affinity chromatography, which exploits the histidine tag attached to the protein for easy isolation.
NDUFS6 participates in redox reactions within Complex I. The iron-sulfur clusters in NDUFS6 undergo oxidation and reduction, facilitating the transfer of electrons from NADH to ubiquinone. This electron transfer is coupled with the translocation of protons across the mitochondrial membrane, contributing to the proton gradient used to produce ATP.
Research on NDUFS6 and other components of Complex I is crucial for understanding mitochondrial diseases and developing potential treatments. Mutations in the NDUFS6 gene can lead to mitochondrial dysfunction, which is associated with various neurodegenerative diseases and metabolic disorders.
