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Alpha Synuclein S87N Mutant Pre-formed Fibrils

Human Recombinant Alpha Synuclein S87N Mutant PFFs

Product Specifications

Background

Human alpha synuclein S87N mutant (HuS87N) has Ser87 mutated to the equivalent mouse residue Asn87, effectively making it a human-mouse chimeric protein. Despite sequence differences at only seven residues, or 5% of the total 140 amino acids, the aggregation rate of wild-type mouse α-syn (MsWT) is faster than wild-type human α-syn (HuWT) in vitro. In wild-type mouse models, MsWT fibrils are more efficient than HuWT fibrils at inducing endogenous mouse α-syn pathology (1) . A53T or S87N substitutions in human α-syn substantially accelerate fibrilization rates in vitro (2,3) . Chimeric HuS87N fibrils show enhanced induction of α-syn pathology greater than both HuWT and MsWT fibrils in mice neuron cultures (4) . Therefore, HuS87N is a good construct for inducing robust endogenous α-syn seeding and pathology in wild-type mice/cultures.

Product Name Alternative

MAPT, 2N4R, Tau40 neurofibrillary tangle protein, paired-helical filament, PHFs, SNCA, NACP, PARK1, asyn, alpha-synuclein, pre-formed fibril, PFFs, mixed fibrils

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

6622

Swiss Prot

P37840-1

Accession Number

NP_000336.1

Expression System

E. coli

Host

E. coli

Origin Species

Human

Target

Alpha Synuclein S87N Mutant

Conjugation

No Tag

Nature

Recombinant

Sequence

MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA

Applications

WB | In vivo Assay | In vitro 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 Purified

Purification

Ion-exchange Purified

Limit Of Detection

Protein certified >95% pure on SDS-PAGE & Nanodrop analysis. Low endotoxin <5 EU/mL @ 2mg/mL.

Concentration

2 mg/ml or 5 mg/ml

Purity

>95%

Weight

0.05

Length

140 AA

Buffer

1X PBS pH 7.4

Molecular Weight

14.46 kDa

Precautions

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

Additionnal Information

For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. Monomer source is catalog# SPR-499.

References & Citations

1. Masuda-Suzukake et al. 2013. Prion-like Spreading of Pathological α-synuclein in Brain. Brain. https://doi.org/10.1093/braiwt037 2. Kang, K. et al. 2011. The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse α-synuclein. JACS. https://doi.org/10.1021/ja203979j 3. Ohgita, T. et al. 2023. Intramolecular Interaction Kinetically Regulates Fibril Formation by Human and Mouse Alpha-Synuclein. Sci Rep https://doi.org/10.1038/s41598-023-38070-4 4. Luk, K., C. et al. 2016. Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity. Cell Rep. https://doi.org/10.1016/j.celrep.2016.08.053

Shipping Conditions

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

Storage Conditions

-80ºC

Notes

For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. Monomer source is catalog# SPR-499.

Protein Length

140 AA

Background Reference 01

1. Masuda-Suzukake et al. 2013. Prion-like Spreading of Pathological α-synuclein in Brain. Brain. https://doi.org/10.1093/brain/awt037 2. Kang, K. et al. 2011. The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse α-synuclein. JACS. https://doi.org/10.1021/ja203979j 3. Ohgita, T. et al. 2023. Intramolecular Interaction Kinetically Regulates Fibril Formation by Human and Mouse Alpha-Synuclein. Sci Rep https://doi.org/10.1038/s41598-023-38070-4 4. Luk, K., C. et al. 2016. Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity. Cell Rep. https://doi.org/10.1016/j.celrep.2016.08.053

AA Sequence

MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA

Immunogen Species

Human

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