Hydrophobicity causes anomalous migration of cystine/glutamate antiporter SLC7A11 in SDS-PAGE with low acrylamide concentration.

ABSTRACT: The cystine/glutamate antiporter, solute carrier family 7 member 11 (SLC7A11), plays a crucial role in regulating redox homeostasis and cell death processes such as apoptosis and ferroptosis. These processes are implicated in various diseases, including cancer, organ injuries and neurodegenerative disorders. However, the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) expression pattern of SLC7A11 varies across studies and remains unclear. In many studies, including ours, SLC7A11 migrates at an atypical molecular weight (MW) of approximately 37 kDa, which is lower than its theoretical molecular mass of 55.4 kDa. This discrepancy raises concerns about the precise molecular mass and expression pattern of SLC7A11 in SDS-PAGE. We confirmed that this fast-migrating band cor

SUBMITTER: Emmanuel N 

PROVIDER: S-EPMC12127883 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature