Recombinant Human beta Synuclein protein (Tag Free)

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Beta-synuclein also known as β-synuclein or SNCB is a protein that plays a role in the nervous system. It is a small protein with a molecular weight around 14 kDa. Predominantly beta-synuclein is found in presynaptic terminals of neurons in the central nervous system including the brain and spinal cord. This protein shares significant amino acid sequence identity with alpha-synuclein and gamma-synuclein comprising the synuclein family. It acts as a modulator of neuronal and synaptic function influencing the dynamics of neurotransmitter release.

Biological function summary

Beta-synuclein contributes to cellular homeostasis and synaptic integrity. It is not typically found as part of a larger protein complex like its relative alpha-synuclein which forms toxic aggregates. Instead beta-synuclein exhibits neuroprotective properties helping maintain neuronal health. It possibly regulates synaptic vesicle cycling and mitigates levels of alpha-synuclein aggregation. Research suggests that loss of beta-synuclein function might disrupt synaptic stability leading to neurological issues.

Pathways

Beta-synuclein engages in synaptic function and plasticity. It participates in pathways related to neurotransmitter release and synaptic vesicle trafficking. Beta-synuclein is connected to calcium/calmodulin-dependent protein kinase II (CaMKII) pathways. This interaction supports beta-synuclein's regulatory impact on synaptic vesicle dynamics negatively modulating the aggregation-prone behaviors seen in alpha-synuclein during synucleinopathies.

Beta-synuclein plays a role in neurodegenerative diseases like Parkinson’s disease and dementia with Lewy bodies. Research highlights its relationship with these conditions due to its interaction with alpha-synuclein known to form pathological aggregates and contribute to disease progression. Beta-synuclein's modulation of alpha-synuclein activity can impact the development and progression of these disorders. There is ongoing interest in its potential protective role suggesting it might be leveraged in therapeutic strategies against synucleinopathy-related diseases.