Recombinant mouse Alpha-synuclein protein Type 1 (Active)
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Recombinant mouse Alpha-synuclein protein Type 1 (Active) is a Mouse Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.
View Alternative Names
Syn, Snca, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP
- FuncS
Supplier Data
Functional Studies - Recombinant mouse Alpha-synuclein protein Type 1 (Active) (AB256155)
Type 1 alpha synuclein preformed fibrils (ab246002) seed the formation of new alpha synuclein fibrils from the pool of alpha synuclein monomers (ab256155). Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha synuclein fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to alpha synuclein protein aggregation) over time when 10 μM of Type 1 alpha synuclein preformed fibrils (ab246002) is combined with 100 μM of alpha synuclein monomer (ab256155), as compared to Type 1 alpha synuclein preformed fibrils (ab246002) or alpha synuclein monomer (ab256155) alone. Thioflavin T ex = 450 nm, em = 485 nm.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant mouse Alpha-synuclein protein Type 1 (Active) (AB256155)
SDS-PAGE - 2μg Mouse Recombinant Alpha-synuclein Protein Monomer (ab256155).
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The alpha-synuclein protein plays critical roles in neuronal activity. It contributes to neurotransmitter release regulation by acting in the formation and plasticity of the presynaptic neuronal network. Alpha-synuclein doesn't usually form parts of large protein complexes but it may associate transiently with membranes and vesicular structures. The protein's monomer form has also been observed in alpha lines and related neuronal processes operating alongside various cellular functions.
Pathways
Synaptic vesicle trafficking and dopamine neurotransmitter release are significant areas involving the alpha-synuclein protein. In these pathways alpha-synuclein interacts with other proteins like synaptophysin and protein monomer monomerizations are intrinsic to these processes. Altered function or aggregation of alpha-synuclein disrupts these pathways influencing broader neurological functions.
Specifications
Form
Liquid
Additional notes
Purified by ion-exchange chromatography.
General info
Function
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed : 20798282, PubMed : 25246573). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity).
Sequence similarities
Belongs to the synuclein family.
Post-translational modifications
Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress.. Ubiquitinated. The predominant conjugate is the diubiquitinated form.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Subcellular localisation
Nucleus
Target data
Product promise
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