Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95% purity, < 5 EU/mL endotoxin level and suitable for FuncS, IHC-P, EM.
>95%
< 5 EU/mL
Escherichia coli
Tag free
FuncS, IHC-P, EM
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 T 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 FuncS | Reactivity Reacts | Dilution info - | Notes - |
Application IHC-P | Reactivity Reacts | Dilution info - | Notes - |
Application EM | 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, NACP, SNCA, PARK1
Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95% purity, < 5 EU/mL endotoxin level and suitable for FuncS, IHC-P, EM.
>95%
< 5 EU/mL
Escherichia coli
Tag free
FuncS, IHC-P, EM
Yes
100 μM ab256149 seeded with 10 μM ab256150 in 25 μM Thioflavin T (PBS pH 7.4, 100 μL reaction volume) generated a fluorescence intensity of 28,000 Relative Fluorescence Units after incubation at 37°C with shaking at 600 rpm for 56 hours. Fluorescence was measured by excitation at 450 nm and emission at 485 nm on a Molecular Devices Gemini XPS microplate reader.
No
Yes
Human
pH: 7.4
Constituents: PBS
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 T 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
14.46 kDa
1 to 140
Recombinant
Liquid
Certified >95% pure using SDS-PAGE analysis.
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
Dry Ice
-80°C
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Preformed type I fibrils.
For best results, sonicate immediately prior to use.
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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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 a limited increase in fluorescence (correlated to alpha synuclein aggregation) over time in A53T alpha synuclein monomers (Recombinant human Alpha-synuclein (mutated A53T) protein monomer Type 1 (Active) ab256149). A much greater increase in fluorescence is seen when 100 μM monomer (Recombinant human Alpha-synuclein (mutated A53T) protein monomer Type 1 (Active) ab256149) is combined with 10 μM of fibrils (ab256150) as the fibrils seed the formation of new fibrils from the pool of active monomers. Thioflavin T ex = 450 nm, em = 485 nm.
Immunohistochemical analysis of primary rat hippocampal neurons showing lewy body inclusion formation when treated with ab256150 (B) but not when treated with a media control (A). Tissue: Primary hippocampal neurons. Species: Sprague-Dawley rat. Primary Antibody: Rabbit anti-pSer129 Antibody. Fibrils were diluted to 1 ug/uL in neuronal media consisting of B27, Glutamax, penicillin/strip, and neurobasalA and sonicated for 1 hour in a water bath. The sonicated stock was then used to achieve the final concentration of 1 ug/mL in the wells.
TEM of ab256150.
TEM of ab256150.
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