{"product_id":"alpha-synuclein-a90c-mutant-monomers-bhp11901235","title":"Alpha Synuclein A90C Mutant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein A90C Mutant Monomers\u003c\/p\u003e\u003cp\u003eThioflavin-T (ThT) fluorescence remains a common measurement of alpha-synuclein fibril formation, yet ThT exhibits poor affinity for oligomers and early aggregates. The alpha-synuclein A90C mutant monomers can be specifically labelled with alternative fluorophores (such as Alexa 488\/Alexa 647) via maleimide chemistry to enable more sensitive FRET analysis of aggregation. The A90C mutant showed no perturbation of monomer structure and Alexa Fluor dye attachment to cysteine 90 was demonstrated to have no effect on the kinetics of fibril formation (1-3). Residue 90 is at the periphery of the NAC region, a key constituent of the alpha-synuclein β-sheet fibril core, which results in fluorophores on different monomers coming into close proximity upon formation of β-sheet structure during aggregation (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length (1 - 140 aa)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 14.49 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM Hepes pH 7.4, 150mM NaCl, 1mM TCEP pH 7.0\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016295407981,"sku":"SPR-478B","price":430.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016295440749,"sku":"SPR-478C","price":770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016295473517,"sku":"SPR-478E","price":1605.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-478_Alpha-Synuclein-A90C-Mutant-Monomers-Protein-FRET-1.png?v=1770644833","url":"https:\/\/www.ebiohippo.com\/products\/alpha-synuclein-a90c-mutant-monomers-bhp11901235","provider":"BioHippo","version":"1.0","type":"link"}