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Proteins and Peptides

Alpha Synuclein TNG (A53T, S87N, N103G) Mutant Monomers

Product Sizes
100 ug
SPR-503-100UG
2 x 100 ug
SPR-503-2X100UG
500 ug
SPR-503-500UG
About this Product
SKU:
SPR-503
Additional Names:
Alpha Synuclein TNG, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, SNCA, PARK1, SYN, PD1, PARK4, Synuclein Alpha, Asyn
Application:
Cell-based/Functional Assay, Western Blot
Buffer:
1X PBS pH7.4
CE/IVD:
RUO
Extra Details:
The TNG variant of alpha-synuclein-comprising A53T, S87N, and N103G mutations-represents a strategically engineered mutant designed to enhance aggregation propensity and mimic disease-relevant biochemical behavior. Human alpha synuclein TNG mutant (HuTNG) is a triple mutant containing Ala53 mutated to the equivalent mouse residue Thr53, Ser87 mutated to the equivalent mouse residue Asn87, and Asn103 mutated to the equivalent mouse residue Gly103, 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 HuTNG fibrils show enhanced induction of A Alpha-syn pathology greater than both HuWT and MsWT fibrils after single unilateral injection into the dorsal striatum in mice (4). Therefore, HuTNG is a good construct for inducing robust endogenous A Alpha-syn seeding and pathology in wild-type mice. TNG mutant monomers serve as a powerful tool for modeling early-stage A Alpha-synuclein pathology. They enable precise investigation of misfolding dynamics, oligomer formation, and cellular toxicity in vitro and in vivo. Their use facilitates the study of molecular mechanisms underlying synaptic dysfunction, mitochondrial impairment, and neuroinflammation-hallmarks of neurodegenerative progression. By replicating key aspects of A Alpha-synuclein-driven disease, TNG mutant monomers support high-throughput screening of therapeutic candidates aimed at stabilizing native protein structure, preventing aggregation, and restoring neuronal function. Their application accelerates translational research targeting Parkinson's disease and related disorders.
Immunogen:
Alpha Synuclein TNG Monomers
Molecular Weight:
14.46 kDa
Purity:
>95%
Purification:
Ion Exchange
Sequence:
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKGEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Shipping Conditions:
Dry Ice
Storage Conditions:
-70[o]C
Supplier:
StressMarq Biosciences
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
SDS-PAGE of purified human alpha synuclein TNG (A53T, S87N, N103G) monomer (SPR-503) on a 12% Bis-Tris Gel. 2ug and 4ug of total protein were loaded into the respective lanes. Electrophoresis was run at 200V for 45 minutes with fixed voltage using 1X MES running buffer.
Fibril formation and seeding activity of human alpha synuclein TNG mutant measured by ThT in vitro. Human TNG mutant monomers (SPR-503) self-aggregate faster than human wild-type monomers. Human TNG mutant pre-formed fibrils (SPR-504) rapidly seed mouse wild-type monomers, but not human wild-type monomers, similar to the seeding pattern observed for mouse wild-type pre-formed fibrils.