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Alpha Synuclein E114C Mutant Monomers: ATTO 488

SKU: BTL-SM-P-00303 | Brand: Stressmarq
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Product Description

Cat Number SPR-517XE-A488
Category Recombinant Protein
Pack Size 500 µg (@5mg/ml)
Description Human Recombinant Alpha Synuclein E114C Mutant Monomers: ATTO 488
Applications WB | Native PAGE | In vitro Assay | In vivo Assay
Target Alpha Synuclein E114C Mutant Monomers: ATTO 488
Molecular Weight 14.434 kDa
Purity >95%
Research Area Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy
Swiss Prot P37840
Scientific 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.
Expression System E.coli
Protein Length 140 aa
Amino Acid Sequence MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILCDMPVDPDNEAYEMPSEEGYQDYEPEA
Purification Ion-exchange & SEC purified
Storage -80ºC
References 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
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Note The product is for research use only
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