Alpha Synuclein A90C Mutant Monomers
Produktgrößen
100 ug
£622,00
SPR-478-100UG
2 x 100 ug
£921,00
SPR-478-2X100UG
5 x 100 ug
£1769,00
SPR-478-5X100UG
Über dieses Produkt
- SKU:
- SPR-478
- Zusätzliche Namen:
- Alpha-synuclein A90C, SNCA, alpha-synuclein, synuclein, Alpha synuclein, NACP, PARK1, PARK4, PD1, Asyn
- Anwendung:
- Cell-based/Functional Assay, Conjugation/Labeling, SDS-PAGE, Western Blot
- Buffer:
- 20mM Hepes pH 7.4, 150mM NaCl, 1mM TCEP pH 7.0
- CE/IVD:
- Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
- Konzentration:
- 2 mg/ml
- Weitere Details:
- The A90C mutation of alpha-synuclein introduces a cysteine residue at position 90, altering the protein's redox sensitivity and structural dynamics. This substitution affects alpha-synuclein's folding behavior and membrane interactions, making the monomeric form of A90C a valuable tool for studying early-stage synucleinopathies. Unlike aggregated species, mutant monomers allow researchers to investigate the initial conformational changes that precede oligomerization and fibril formation. Thioflavin-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. Residue 90 is at the periphery of the NAC region, a key constituent of the alpha-synuclein B Beta-sheet fibril core, which results in fluorophores on different monomers coming into proximity upon formation of B Beta-sheet structure during aggregation. Note: To prevent the potential mistranslation of alpha-synuclein Y136 as C136 during E.coli expression, the Y136-TAT construct was used. By modeling the earliest molecular disruptions in alpha-synuclein biology, A90C mutant monomers provide a precise and disease-relevant platform for advancing neurodegenerative research and accelerating the development of preventative interventions. Thioflavin-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 B Beta-sheet fibril core, which results in fluorophores on different monomers coming into close proximity upon formation of B Beta-sheet structure during aggregation. Note: To prevent the potential mis-translation of alpha-synuclein Y136 as C136 during E.coli expression, the Y136-TAT construct was used.
- Immunogen:
- Alpha Synuclein A90C Monomers
- Molekulargewicht:
- 14.49 kDa
- Reinheit:
- >95%
- Aufreinigung:
- Ion Exchange
- Sequenz:
- MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIACATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
- Versandbedingungen:
- Dry Ice
- Lagerbedingungen:
- -70[o]C
- Hersteller:
- StressMarq Biosciences
- Typ:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
- Datenblatt des Herstellers:https://www.stressmarq.com/products/protein/alpha-synuclein-a90c-mutant-monomers-spr-478/