Transthyretin Amyloidosis (ATTR)

Transthyretin amyloidosis (ATTR) is a rare disease characterized by the abnormal accumulation of amyloid deposits made up of misfolded transthyretin (TTR) proteins in various organs, including the retina, vitreous, kidneys, and brain. Two prominent subtypes are transthyretin amyloid polyradiculoneuropathy (ATTR-PN) and transthyretin amyloid cardiomyopathy (ATTR-CM).

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Mouse Models Related to Neurological Diseases
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Studies Completed
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ND-Enabling Studies

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Human TTR Expression Platforms

Our models express human TTR (wild-type or V30M mutant), enabling accurate evaluation of TTR-targeting therapies in a species-compatible system with clinically relevant pathology.

Versatile Model Options

Our ATTR model panel spans knock-in and transgenic models — with or without Ttr knockout — supporting research across TTR secretion kinetics, amyloid deposition, and beyond.

Translational Readouts

Serum human TTR quantification by ELISA, tissue amyloid assessment, and organ-specific pathology endpoints are available to characterize therapeutic efficacy in ATTR models.

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Case Studies & Validation Data

Human TTR Expression Validation Study

Human TTR Protein Expression in B6-hTTR V30M Tg Mice Confirmed by ELISA

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Human TTR Protein Expression in B6-hTTR V30M Tg Mice Confirmed by ELISA

The expression levels of human TTR protein in the serum of wild-type (WT Ctrl) and B6-hTTRV30M Tg mice were detected by ELISA, with human serum serving as a positive control. Human TTR protein was successfully expressed in the serum of B6-hTTRV30M Tg mice, whereas no expression was detected in wild-type mice.

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Transthyretin Amyloidosis (ATTR)

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