Recombinant human Alpha-Synuclein protein filament is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95% purity, < 0.1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS, Dot, sELISA.
>95% SDS-PAGE
< 0.1 EU/µg
Escherichia coli
Tag free
SDS-PAGE, FuncS, Dot, sELISA
Yes
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 E 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 |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Application Dot | Reactivity Reacts | Dilution info - | Notes - |
Application sELISA | 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. 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). Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590).
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PARK1, NACP, SNCA
Recombinant human Alpha-Synuclein protein filament is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95% purity, < 0.1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS, Dot, sELISA.
>95% SDS-PAGE
< 0.1 EU/µg
Escherichia coli
Tag free
SDS-PAGE, FuncS, Dot, sELISA
Yes
Functional in a thioflavin binding assay.
>x100 signal when compared to monomer control.
No
Human
Resuspend in water. Lyophilized contents may appear as either a translucent film or a white powder. This variance does not affect the quality of the product.
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 E 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
1 to 140
Recombinant
Lyophilized
Purity >95% by LC/MS
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. 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). Plays also 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
Ambient - Cannot Ship with Ice
Ambient
Ambient
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Alpha-Synuclein is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals. The deposition of the abundant presynaptic brain protein alpha-synuclein as fibrillary aggregates in neurons or glial cells is a hallmark lesion in a subset of neurodegenerative disorders. These disorders include Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy, collectively referred to as synucleinopathies. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin.
This antibody was developed with support from The Michael J. Fox Foundation.
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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Sandwich ELISA - Recombinant human Alpha-Synuclein protein filament standard curve
Background subtracted standard curve using Human Alpha-synuclein Antibody Pair - BSA and Azide free (Human Alpha-synuclein Antibody Pair - BSA and Azide free ab270346) and Recombinant human Alpha-Synuclein protein filament (ab254309) in sandwich ELISA. The ELISA was performed using the components of the corresponding SimpleStep® kit, which uses the same antibody pair with a different formulation and format.
Thioflavin binding by ab254309.
Functional in a thioflavin binding assay.
>x100 signal when compared to monomer control.
SDS-PAGE analysis of ab254309.
Confirmation specific Antibody binding.
Positive signal when assayed by Dotblot, binding Anti-Alpha-synuclein aggregate antibody [MJFR-14-6-4-2] - Conformation-Specific ab209538.
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