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Spastin is an ATP-dependent microtubule-severing protein and a member of the ATPases associated with various cellular activities (AAA) family encoded by SPG4 in humans.1 It is composed of a hydrophobic region, microtubule-interacting and endosomal trafficking (MIT) domain, microtubule-binding domain, and an AAA ATPase domain.2,3 It is ubiquitously expressed and localized to the endoplasmic reticulum. Alternative splicing of SPG4 produces a second shorter isoform that lacks the first 87 amino acids of full-length spastin and is localized to the cytosol.4 Spastin functions as a hexamer that binds to tubulin dimers on the plus-end of microtubules and disrupts tubulin dimer interactions in an ATP-dependent manner to sever them from microtubules.5 Mutations in SPG4 are associated with autosomal dominant uncomplicated hereditary spastic paraplegia (HSP).2,4 Cayman’s Spastin (N-Term) Rabbit Monoclonal Antibody (Clone RM346) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Spastin depletion increases tubulin polyglutamylation and impairs kinesin-
2. Spastin MIT domain disease-
3. Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics. Hum. Mol. Genet. 11(2), 153-163 (2002).
4. Functional differences of short and long isoforms of spastin harboring missense mutation. Dis. Model Mech. 11(9), dmm033704 (2018).
5. Microtubule-