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. [provided by RefSeq, Jul 2008],
Immunohistochemical analysis of paraffin-embedded human Gastric adenocarcinoma. 1, Antibody was diluted at 1:200(4 overnight). 2, Tris-EDTA,pH9.0 was used for antigen retrieval. 3,Secondary antibody was diluted at 1:200(room temperature, 45min).
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