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Alpha Synuclein E114C Mutant Monomers: ATTO 488

Human Recombinant Alpha Synuclein E114C Mutant Monomers: ATTO 488

Product Specifications

Background

The alpha-synuclein (aSyn) E114C mutation facilitates a single site-specific conjugation with ATTO-488 maleimide that avoids any hindrance on fibrilization or cell entry that may be conferred by non-specific lysine targeting conjugations. This conjugation is ideal due to internal position relative to C-terminal truncation sites, proximity to the NAC, and lack of interference with recruitment in vitro or in primary neurons (1, 2) . Pre-formed fibrils (PFFs) generated with 5-25% fluorescently tagged E114C mutants have demonstrated a relative potency >80% compared to wild-type aSyn for inducing misfolding of endogenous aSyn, indicating no significant perturbation of seeding in living cells (1) . Atto-488 is a useful tool for identifying cell entry, as the addition of Trypan Blue to cultures prior to imaging will quench fluorescence of extracellular Atto-488 conjugated aSyn (3) . Our aSyn E114C-Atto-488 PFFs, which contain 10% fluorescently tagged E114C mutants, are an excellent tool for studying cell entry and localization, with demonstrated entry into neurons after trypan blue quenching.

Product Name Alternative

Alpha synuclein monomer, Alpha-synuclein monomer, Alpha synuclein protein monomer, Alpha synuclein monomer, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, Alpha synuclein monomers, SYN protein, Parkinson's disease familial 1 Protein

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Swiss Prot

P37840

Expression System

E. coli

Host

E.coli

Origin Species

Human

Target

Alpha Synuclein E114C Mutant Monomers: ATTO 488

Conjugation

ATTO 488

Nature

Recombinant

Sequence

MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILCDMPVDPDNEAYEMPSEEGYQDYEPEA

Applications

WB | Native PAGE | In vitro Assay | In vivo Assay

Field of Research

Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy

Purification Method

Ion-exchange & SEC purified

Purification

Ion-exchange & SEC purified

Limit Of Detection

Protein certified >95% pure on SDS-page and nanodrop analysis, endotoxin below 5 EU/mL at 2 mg/mL

Concentration

Lot/batch specific. See included datasheet.

Purity

>95%

Weight

0.05

Length

140 aa

Buffer

1X PBS pH 7.4

Molecular Weight

14.434 kDa

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

Additionnal Information

For corresponding PFFs, see catalog# SPR-518-A488

References & Citations

1. Haney et al. 2016. Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis. Organic & Biomolecular Chemistry. DOI: 10.1039/c5ob02329g 2. Karpowicz et al. 2017. Selective imaging of internalized proteopathic a-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies. JBC. DOI: 10.1074/jbc.M117.780296 3. Pieri et al. 2016. Structural and functional properties of prefibrillar α-synuclein oligomers. Scientific Reports. DOI: 10.1038/srep24526

Shipping Conditions

Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.

Storage Conditions

-80ºC

Notes

For corresponding PFFs, see catalog# SPR-518-A488

Protein Length

140 aa

Background Reference 01

1. Haney et al. 2016. Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis. Organic & Biomolecular Chemistry. DOI: 10.1039/c5ob02329g 2. Karpowicz et al. 2017. Selective imaging of internalized proteopathic a-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies. JBC. DOI: 10.1074/jbc.M117.780296 3. Pieri et al. 2016. Structural and functional properties of prefibrillar α-synuclein oligomers. Scientific Reports. DOI: 10.1038/srep24526

AA Sequence

MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILCDMPVDPDNEAYEMPSEEGYQDYEPEA

Immunogen Species

Human

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