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


The Alpha Synuclein TNG (A53T-S87N-N103G) Mutant Monomers are intended for research use only and not for use in diagnostic or clinical procedures. Contact us for bulk pricing.

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

The Alpha Synuclein TNG (A53T-S87N-N103G) Mutant Monomers are For Research Use Only

Specificity: N/A
Species: Human
Expression System: E. coli
Buffer: 1X PBS pH7.4
Storage Temperature: -80ºC
Alternative Names: Alpha synuclein protein, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkinson’s disease familial 1 Protein, Alpha Synuclein TNG

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Scientific Background

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 α-syn (MsWT) is faster than wild-type human α-syn (HuWT) in vitro. In wild-type mouse models, MsWT fibrils are more efficient than HuWT fibrils at inducing endogenous mouse α-syn pathology. A53T or S87N substitutions in human α-syn substantially accelerate fibrilization rates in vitro. Chimeric HuTNG fibrils show enhanced induction of α-syn pathology greater than both HuWT and MsWT fibrils after single unilateral injection into the dorsal striatum in mice. Therefore, HuTNG is a good construct for inducing robust endogenous α-syn seeding and pathology in wild-type mice.

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