SLC7A11 Protein, Human (Cell-Free, His)

SLC7A11 Protein, forming a heterodimer with SLC3A2, operates as an antiporter, facilitating the exchange of extracellular anionic L-cystine for intracellular L-glutamate across the cellular plasma membrane. This sodium-independent, electroneutral transport, with a stoichiometry of 1:1, is propelled by the high intracellular concentration of L-glutamate and the intracellular reduction of L-cystine. The pivotal role of SLC7A11 extends to providing L-cystine for maintaining the redox balance between extracellular L-cystine and L-cysteine, essential for cellular protection against oxidative stress. Additionally, it mediates the import of L-kynurenine, contributing to anti-ferroptotic signaling that is crucial for L-cystine and glutathione homeostasis. Furthermore, SLC7A11 facilitates N-acetyl-L-cysteine uptake into the placenta, leading to the down-regulation of oxidative stress, inflammation, and apoptosis-associated pathways. In vitro, the protein exhibits the ability to transport L-aspartate. Beyond its transport functions, SLC7A11 may play a role in astrocyte and meningeal cell proliferation during development, offering neuroprotection by promoting glutathione synthesis and delivery from non-neuronal cells, such as astrocytes and meningeal cells, to immature neurons. Notably, it controls the direct production of pheomelanin pigment.