Recombinant Human CHMP2A protein

CHMP2A (Charged Multivesicular Body Protein 2A) is a key component of the Endosomal Sorting Complex Required for Transport (ESCRT) machinery, which regulates essential membrane remodeling processes in eukaryotic cells. As part of the ESCRT-III subcomplex, CHMP2A plays a critical role in membrane scission events, including multivesicular body (MVB) formation, cytokinesis, viral budding, and plasma membrane repair. It functions by forming helical filaments that constrict membranes, often in coordination with the AAA+ ATPase VPS4. which disassembles the filaments to complete membrane fission.

Structurally, CHMP2A contains a characteristic N-terminal basic domain and a C-terminal α-helical region. The protein undergoes conformational changes to transition from a soluble monomer to a membrane-bound polymerized state, a process regulated by interactions with other ESCRT components like CHMP4B. Notably, CHMP2A shares homology with CHMP2B, an isoform linked to neurodegenerative disorders, but differs in regulatory roles and tissue expression patterns.

Recombinant CHMP2A proteins are widely used to study ESCRT-III assembly mechanisms, membrane dynamics, and disease pathology. In research, purified CHMP2A enables in vitro reconstitution of membrane scission events, structural analysis (e.g., cryo-EM), and screening for inhibitors targeting ESCRT dysfunction. Dysregulation of CHMP2A has been implicated in cancer metastasis, neurological diseases, and defective cellular clearance pathways, making it a potential biomarker or therapeutic target. Its recombinant form is typically expressed in bacterial or mammalian systems with tags (e.g., His-tag) for purification and detection.