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Proteins and Peptides

Alpha Synuclein S87N Mutant Pre-formed Fibrils

Product Sizes
100 ug
SPR-500-100UG
2 x 100 ug
SPR-500-2X100UG
5 x 100 ug
SPR-500-5X100UG
500 ug
SPR-500-500UG
2 x 500 ug
SPR-500-2X500UG
About this Product
SKU:
SPR-500
Additional Names:
MAPT, 2N4R, Tau40 neurofibrillary tangle protein, paired-helical filament, PHFs, SNCA, NACP, PARK1, asyn, alpha-synuclein, pre-formed fibril, PFFs, mixed fibrils
Application:
Cell-based/Functional Assay, Western Blot
Extra Details:
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 A Alpha-syn (MsWT) is faster than wild-type human A Alpha-syn (HuWT) in vitro. In wild-type mouse models, MsWT fibrils are more efficient than HuWT fibrils at inducing endogenous mouse A Alpha-syn pathology (1). A53T or S87N substitutions in human A Alpha-syn substantially accelerate fibrilization rates in vitro (2,3). Chimeric HuS87N fibrils show enhanced induction of A Alpha-syn pathology greater than both HuWT and MsWT fibrils in mice neuron cultures (4). Therefore, HuS87N is a good construct for inducing robust endogenous A Alpha-syn seeding and pathology in wild-type mice/cultures.
Molecular Weight:
14.46 kDa
Purity:
>95%
Purification:
Ion Exchange
Sequence:
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Shipping Conditions:
Dry Ice
Storage Conditions:
-70[o]C
Supplier:
StressMarq Biosciences
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
TEM of human alpha synuclein S87N fibrils (SPR-500). Negative stain transmission electron microscopy images acquired at 80 Kv on carbon coated 400 mesh copper grids using phosphotungstic acid and uranyl acetate stain. Scale bar = 200 nm. Method: Samples were prepared for examination in the transmission electron microscope using the 'direct application method' (Doane and Anderson 1987).
SDS-PAGE of human alpha synuclein S87N fibrils (SPR-500) under reducing conditions showing the protein purity. Lane 1: Biorad All Blue Standards (3uL), Lane 2: human alpha synuclein S87N pre-formed fibrils (2ug), lane 3: human alpha synuclein S87N pre-formed fibrils (4ug).
Fibril formation activity of human alpha synuclein S87N mutant monomers (SPR-499) seeded by human alpha synuclein S87N mutant pre-formed fibrils (SPR-500). The graph shows an increase in ThT signal indicating increased beta-sheet content and fibril formation over 72 hours.
Sedimentation assay of human alpha synuclein S87N fibrils showing >90% of material is insoluble when spun at 20,000 xg. Lane 1: Biorad All Blue Standards (3uL), Lanes 2-4: human alpha synuclein S87N pre-formed fibrils (10ug) supernatant, wash and pellet.
TEM of human alpha synuclein S87N fibrils (SPR-500). Negative stain transmission electron microscopy images acquired at 80 Kv on carbon coated 400 mesh copper grids using phosphotungstic acid and uranyl acetate stain. Scale bar = 100 nm. Method: Samples were prepared for examination in the transmission electron microscope using the 'direct application method' (Doane and Anderson 1987).