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AB256150

Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active)

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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%, < 5 EU/mL endotoxin level, suitable for SDS-PAGE, WB, FuncS, EM.

View Alternative Names

NACP, PARK1, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor

4 Images
Functional Studies - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)
  • FuncS

Supplier Data

Functional Studies - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)

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 (ab256149). A much greater increase in fluorescence is seen when 100 μM monomer (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.

Electron Microscopy - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)
  • EM

Supplier Data

Electron Microscopy - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)

TEM of ab256150.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)

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.

Electron Microscopy - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)
  • EM

Supplier Data

Electron Microscopy - Recombinant Human Alpha-synuclein (mutated A53T) protein aggregate Type 1 (Active) (AB256150)

TEM of ab256150.

Key facts

Purity

>95%

Endotoxin level

< 5 EU/mL

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, FuncS, WB, EM

applications

Biologically active

Yes

Biological activity

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.

Accession

P37840

Animal free

No

Carrier free

Yes

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS

storage-buffer

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Primary Antibodies

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "EM": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Preformed type I fibrils.

For best results, sonicate immediately prior to use.

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Sequence info

[{"sequence":"MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA","proteinLength":"Full Length","predictedMolecularWeight":"14.46 kDa","actualMolecularWeight":null,"aminoAcidEnd":140,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P37840","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
True
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Supplementary information

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.
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.

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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Specifications

Form

Liquid

Additional notes

Certified >95% pure using SDS-PAGE analysis.

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General info

Function

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). Also acts 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).

Sequence similarities

Belongs to the synuclein family.

Post-translational modifications

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.. Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.. Ubiquitinated. The predominant conjugate is the diubiquitinated form.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.

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Product protocols

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Target data

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). Also acts 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).
See full target information SNCA mutated A53T
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