Background

The human NDUFA1 gene codes for an essential component of complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha-helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and might act as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane. However, the NDUFA1 peptide is one of about 31 components of the “hydrophobic protein” (HP) fraction of complex I which is involved in proton translocation. Thus the NDUFA1 peptide may also participate in that function.

Images

	Western blotting analysis using anti-NDUFA1 antibody (Cat#64905). Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with anti-NDUFA1 antibody (Cat#64905, 1:5,000) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using FeQ™ ECL Substrate Kit (Cat#226).
	Western blotting analysis using anti-NDUFA1 antibody (Cat#64905). NDUFA1 expression in wild-type (WT) and NDUFA1 knockdown (KD) HSHC cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with anti-NDUFA1 antibody (Cat#64905, 1:5,000) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using FeQ™ ECL Substrate Kit (Cat#226).
	Flow cytometric analysis of NDUFA1 expression in HepG2 cells using anti-NDUFA1 antibody (Cat#64905, 1:2,000). Green, isotype control; red, NDUFA1.

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