Recombinant Human HOMER2 protein

HOMER2 is a member of the HOMER family of scaffolding proteins, which play critical roles in organizing synaptic signaling complexes and regulating intracellular calcium dynamics. These proteins are evolutionarily conserved and characterized by two primary domains: an N-terminal Enabled/VASP homology 1 (EVH1) domain that binds proline-rich motifs in target proteins, and a C-terminal coiled-coil domain enabling self-oligomerization. HOMER2 exists in multiple splice variants, including the short forms (e.g., HOMER2a) that act as dominant-negative regulators and the long forms (e.g., HOMER2b) that facilitate protein clustering.

Functionally, HOMER2 interacts with metabotropic glutamate receptors (mGluRs), inositol trisphosphate receptors (IP3Rs), and other signaling molecules, bridging membrane receptors to intracellular effectors. It modulates synaptic plasticity, neurotransmitter release, and calcium homeostasis, particularly in brain regions like the striatum and hippocampus. Studies implicate HOMER2 in neuropsychiatric conditions, including addiction and cognitive disorders. For example, HOMER2 knockout mice exhibit altered behavioral responses to psychostimulants, highlighting its role in reward pathways.

Recombinant HOMER2 proteins are engineered to study these mechanisms *in vitro* or *in vivo*. Produced via bacterial or mammalian expression systems, they often include tags (e.g., His, GFP) for purification and tracking. Researchers use these proteins to dissect domain-specific interactions, reconstitute signaling pathways, or rescue phenotypes in HOMER2-deficient models. Recent work also explores its involvement in neurodegenerative diseases, such as Alzheimer’s, where disrupted calcium signaling may contribute to pathology. By enabling precise manipulation of HOMER2 interactions, recombinant forms advance our understanding of synaptic dysfunction and therapeutic targeting.