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SNPH is a stress-regulated mitochondrial switch of the cell proliferation-motility balance in cancer, and its pathway may represent a therapeutic target.
Stressed mitochondria are removed from axons triggered by the bulk release of mitochondrial anchoring protein syntaphilin via a new class of mitochondria-derived cargos independent of Parkin (zeige PARK2 ELISA Kits), Drp1 (zeige CRMP1 ELISA Kits), and autophagy.
syntaphilin is an inhibitor of both SNARE (zeige NAPA ELISA Kits)-based fusion and dynamin (zeige DNM1 ELISA Kits)-mediated endocytosis
SNPH deletion produces striking benefits in the Shiverer (zeige MBP ELISA Kits) mouse by prolonging survival, reducing cerebellar damage, suppressing oxidative stress, and improving itochondrial health.
syntaphilin expression in astrocytes at the optic nerve might be involved in axonal injury.
SNPH is required for activity-dependent regulation of mitochondrial transport.
Here, we report a role for axon-targeted syntaphilin (SNPH) in mitochondrial docking through its interaction with microtubules. Axonal mitochondria that contain exogenously or endogenously expressed SNPH lose mobility.
Our studies suggest an unexpected role for LC8 (zeige DYNLL1 ELISA Kits) and provide new mechanistic insights into how SNPH and LC8 (zeige DYNLL1 ELISA Kits) together immobilize mitochondria through a dynamic interaction between the docking receptor and axonal cytoskeleton.
Syntaxin-1, synaptobrevin/VAMP, and SNAP25 interact to form the SNARE complex, which is required for synaptic vesicle docking and fusion. The protein encoded by this gene is membrane-associated and inhibits SNARE complex formation by binding free syntaxin-1. Expression of this gene appears to be brain-specific.