Serine racemase (SRR) is an enzyme that catalyzes the conversion of L-serine to D-serine, a co-agonist of N-methyl-D-aspartate (NMDA) receptors critical for glutamatergic neurotransmission. Dysregulation of D-serine levels, mediated by SRR, has been implicated in neuropsychiatric and neurodegenerative disorders, including schizophrenia, Alzheimer’s disease, and ischemic brain injury. Antibodies targeting SRR are essential tools for studying its expression, localization, and functional roles in both physiological and pathological contexts.
SRR antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to map SRR distribution in brain tissues, particularly in astrocytes and neurons. They help elucidate SRR’s involvement in synaptic plasticity, neuroinflammation, and excitotoxicity. Additionally, these antibodies aid in investigating post-translational modifications (e.g., phosphorylation) and interactions with binding partners, such as GRIP1. which regulate SRR activity.
Commercial SRR antibodies are typically raised against specific epitopes (e.g., human or murine SRR fragments) and validated for species cross-reactivity. Challenges include ensuring specificity due to SRR’s structural homology with other serine dehydratases. Recent studies leverage SRR antibodies to explore therapeutic strategies, such as modulating D-serine levels in disease models. Overall, SRR antibodies remain pivotal in advancing understanding of glutamate signaling pathways and developing targeted interventions for neurological disorders.