SNCB Human

Beta-synuclein is an acidic neuronal protein composed of 134 amino acids. It is known for its extreme heat resistance and chaperone-like activity . The recombinant form of human beta-synuclein is typically produced in E. coli and is available as an un-tagged protein . The amino acid sequence of beta-synuclein is as follows:

MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTREGVVQ GVASVAEKTK EQASHLGGAV FSGAGNIAAA TGLVKREEFP TDLKPEEVAQ EAAEEPLIEP LMEPEGESYE DPPQEEYQEY EPEA

The predicted molecular mass of beta-synuclein is approximately 14.2 kDa, although the observed molecular weight may vary due to post-translational modifications and other experimental factors .

Beta-synuclein is primarily found in brain tissue, particularly in presynaptic terminals. It is predominantly expressed in regions such as the neocortex, hippocampus, striatum, thalamus, and cerebellum . Unlike alpha-synuclein, beta-synuclein is not found in Lewy bodies, which are characteristic of Parkinson’s disease and dementia with Lewy bodies. However, it is associated with hippocampal pathology in these conditions .

Beta-synuclein plays a crucial role in maintaining synaptic function and plasticity. It has been suggested to inhibit the aggregation of alpha-synuclein, which is implicated in neurodegenerative diseases such as Parkinson’s disease . Additionally, beta-synuclein has been shown to have chaperone-like activity, helping to stabilize other proteins and prevent their misfolding .

Recombinant human beta-synuclein is widely used in research to study its structure, function, and role in neurodegenerative diseases. It is also used to investigate potential therapeutic strategies for conditions involving synucleinopathies. The protein is typically supplied in a buffer solution and should be stored at -20°C for long-term stability .