Introducing the recombinant SRA stem-loop-interacting RNA-binding protein, mitochondrial (SLIRP) fragment (residues 1-109), a high-purity tool designed for studying RNA-binding mechanisms and nuclear receptor corepressor functions. This fragment fully encompasses the RRM domain, making it ideal for targeted investigations into SLIRP's molecular interactions.

The full-length SLIRP protein, encoded by the SLIRP gene in Homo sapiens, functions as an RNA-binding protein and nuclear receptor corepressor. It binds specifically to the SRA RNA, repressing SRA-mediated coactivation of nuclear receptors, and has been shown to inhibit transactivation by glucocorticoid (GR), androgen (AR), thyroid (TR), and vitamin D (VDR) receptors. SLIRP localizes predominantly to the mitochondrion, with a fraction present in the nucleus, where it is recruited to nuclear receptor target promoters, highlighting its dual role in transcriptional regulation and mitochondrial processes.