The Gem-associated protein 2 (GEMIN2), also known as SIP1. is a critical component of the survival motor neuron (SMN) complex, which plays essential roles in small nuclear ribonucleoprotein (snRNP) assembly, pre-mRNA splicing, and neuronal function. GEMIN2 directly interacts with SMN, forming a stable core of the multi-protein complex required for the biogenesis of spliceosomal snRNPs. Antibodies targeting GEMIN2 are widely used to study the molecular composition and dynamics of the SMN complex, particularly in the context of spinal muscular atrophy (SMA), a neurodegenerative disorder linked to SMN1 gene mutations. These antibodies enable researchers to investigate GEMIN2-SMN interactions, monitor complex stability, and assess cellular localization via techniques like Western blotting, immunoprecipitation, and immunofluorescence. Commercially available GEMIN2 antibodies are typically raised against specific epitopes within its conserved regions, often validated for cross-reactivity in human, mouse, and other model organisms. Studies utilizing GEMIN2 antibodies have revealed its role in snRNA chaperoning, stress granule formation, and potential contributions to broader RNA metabolism pathways beyond splicing. Dysregulation of GEMIN2 expression or interactions is increasingly explored in neuromuscular diseases and cancer, highlighting its broader biological significance. Proper validation of GEMIN2 antibodies remains crucial due to shared epitopes among SMN complex proteins and splice variants.