Recombinant Human Alpha-synuclein (mutated E46K) protein is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
Escherichia coli
Tag free
SDS-PAGE
No
M D V F M K G L S K / A K E G V V A A A E / K T K Q G V A E A A / G K T K E G V L Y V / G S K T K [ K ] G V V H / G V A T V A E K T K / E Q V T N V G G A V / V T G V T A V A Q K / T V E G A G S I A A / A T G F V K K D Q L / G K N E E G A P Q E / G I L E D M P V D P / D N E A Y E M P S E / E G Y Q D Y E P E A
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:20798282, PubMed:26442590, PubMed:28288128, PubMed:30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). 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). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590).
NACP, PARK1, PARK1, NACP, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP
Recombinant Human Alpha-synuclein (mutated E46K) protein is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
Escherichia coli
Tag free
SDS-PAGE
No
No
Human
pH: 7.5
Constituents: 0.58% Sodium chloride, 0.316% Tris HCl
M D V F M K G L S K / A K E G V V A A A E / K T K Q G V A E A A / G K T K E G V L Y V /
G S K T K [ K ] G V V H / G V A T V A E K T K / E Q V T N V G G A V / V T G V T A V A Q K / T V E G A G S I A A /
A T G F V K K D Q L / G K N E E G A P Q E / G I L E D M P V D P / D N E A Y E M P S E / E G Y Q D Y E P E A
Full Length
14.4 kDa
1 to 140
Recombinant
Liquid
Alpha Synuclein E46K was overexpressed in *E. coli* and purified to apparent homogeneity by using conventional column chromatography techniques.
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:20798282, PubMed:26442590, PubMed:28288128, PubMed:30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). 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). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590).
Belongs to the synuclein family.
Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.
Nucleus
Blue Ice
-20°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Recent studies have shown that this mutant(E46K) of alpha-synuclein causes Parkinson and Lewy Body dementia(DLB).
This supplementary information is collated from multiple sources and compiled automatically.
Alpha-synuclein often referred to by alternate names such as SNCA is a protein of around 14 kDa mass. It mainly expresses in the brain particularly in presynaptic nerve terminals. This protein functions mechanically by stabilizing synaptic vesicles and maintaining synaptic function. It exists both in soluble monomer forms and as aggregates in protein filaments. Antibodies like 4D6 and EP1536Y target monomer forms of protein for more detailed studies.
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.
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.
Alterations or accumulations of alpha-synuclein are strongly linked to Parkinson's disease and Lewy body dementia. In these conditions alpha-synuclein forms abnormal protein filaments known as Lewy bodies within neurons. These formations disrupt cellular processes and neuron health. Synucleinopathies such as these show connections with proteins like parkin and DJ-1 which also have key roles in these neurodegenerative diseases.
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ab51188 in 15%SDS-PAGE
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