Recombinant Human CPLX3 protein (His tag) is a Human Fragment protein, in the 1 to 154 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
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Nbla11589, CPLX3, Complexin-3, Complexin III, CPX III
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human CPLX3 protein (His tag) (AB276620)
SDS-PAGE analysis of ab276620
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This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Complexin-3 participates in synaptic vesicle exocytosis by binding to the SNARE complex. This interaction helps regulate the release of neurotransmitters which is essential for proper synaptic function. CPLX3 plays a part in the synaptic vesicle cycle and ensures the precise timing of neurotransmitter release. It may also modulate synaptic plasticity which influences learning and memory processes in the CNS.
Pathways
Complexin-3 operates within the synaptic vesicle cycle and neurotransmitter release pathways. It collaborates closely with SNARE proteins like Syntaxin and Synaptobrevin both key for membrane fusion and neurotransmitter release. CPLX3 fine-tunes these processes impacting the efficiency and dynamics of synaptic transmission. Its function in these pathways highlights its relevance in regulating synaptic communication and plasticity.
일반 정보
기능
Complexin that regulates SNARE protein complex-mediated synaptic vesicle fusion (By similarity). Required for the maintenance of synaptic ultrastructure in the adult retina (By similarity). Positively regulates synaptic transmission through synaptic vesicle availability and exocytosis of neurotransmitters at photoreceptor ribbon synapses in the retina (By similarity). Suppresses tonic photoreceptor activity and baseline 'noise' by suppression of Ca(2+) vesicle tonic release and the facilitation of evoked synchronous and asynchronous Ca(2+) vesicle release (By similarity).
서열 유사성
Belongs to the complexin/synaphin family.
Post-translational modifications
Farnesylation mediates presynaptic targeting.
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