Amprion, Inc.

Yihua Ma

Luis Concha

Carly Farris

Bret Holguin

Hieu Huu Nguyen

Inert matrices for use with α-synuclein seed amplification assays (αS-SAAs) are provided. The inert matrices accurately reflect the absence of misfolded αS protein when used as a negative control, in the form of no, perceptively low, or delayed αS substrate self-aggregation, yet will readily permit aggregation of the αS substrate with seeds when used as a positive control. The inert matrices may be used to screen for αS-SAA reagent competence. The inert matrices may be used to dilute samples taken from peripheral biological matrices. Finally, the inert matrices may be used as a diluent for serial dilutions of αS-SAA samples, to enable semi-quantitative versions of αS-SAAs.

Inert matrices for qualitative and semi-quantitative seed amplification assays

An expression vector is provided for production of human alpha-synuclein (αS) protein or a conservative variant thereof that exhibits a decreased tendency to self-aggregate in an αS seed amplification assay (SAA). The expression vector comprises a nucleic acid sequence coding for human αS protein or a conservative variant, the nucleic acid sequence comprising codons that have been optimized to produce human αS protein or a conservative variant when expressed by a host cell such as. The codons have been optimized to avoid amino acid misincorporation in the expressed protein. Methods for purification of the expressed protein are also provided.

Alpha-synuclein substrates and methods for making and using the same

An expression vector is provided for production of human alpha-synuclein (&#x3b1;S) protein or a conservative variant thereof that exhibits a decreased tendency to self-aggregate in an &#x3b1;S seed amplification assay (SAA). The expression vector comprises a nucleic acid sequence coding for human &#x3b1;S protein or a conservative variant, the nucleic acid sequence comprising codons that have been optimized to produce human &#x3b1;S protein or a conservative variant when expressed by a host cell such as. The codons have been optimized to avoid amino acid misincorporation in the expressed protein. Methods for purification of the expressed protein are also provided.

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Corona, CA, United States of America

Yihua Ma