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Amyloidosis is a collective term for a group of diseases characterized by the deposition of abnormal proteins in tissues. Our company is committed to developing cutting-edge diagnostics and therapeutics for managing amyloidosis. As your reliable partner in amyloidosis research, we offer streamlined and comprehensive solutions to meet all your scientific research requirements.

Introduction to Amyloidosis

Amyloidosis is a group of rare and complex disorders that affects various organs and tissues in the body. It is characterized by the accumulation of misshapen proteins known as amyloid fibrils, which disrupt normal organ function and can lead to organ failure. The overall prevalence of amyloidosis is estimated to be 30 cases per 100,000 individuals.

An overview diagram of the molecular mechanisms of cardiotoxicity in AL amyloidosis.Fig. 1 Molecular mechanisms of cardiotoxicity in AL amyloidosis. (Ikura, Hidehiko, et al., 2022)

Pathogenesis of Amyloidosis

Protein misfolding results in the formation of amyloid fibrils. These fibrils accumulate in various organs, leading to organ dysfunction and the development of amyloidosis. The exact mechanism of amyloid fibril formation is still under investigation, but several key proteins have been identified in common types of amyloidosis.

Disease Type Fibril Protein Affected Organs Incidence
AL amyloidosis Immunoglobulin light chains (AL) Heart, kidneys, and other organs 12/1,000,000
AA amyloidosis Serum A protein Kidneys, liver, and gastrointestinal tract 1-2/1,000,000
ATTR amyloidosis Transthyretin (TTR) protein heart and nervous system 1/5,800

Strategies of Amyloidosis Therapy Development

Reduce Abnormal Protein Production

The underlying cause of amyloidosis is the abnormal production of specific proteins. In the case of AL amyloidosis, the production of abnormal light chains can be decreased through the use of chemotherapy regimens, immunomodulatory drugs, or proteasome inhibitors.

Inhibit Protein Misfolding and Aggregation

Preventing protein misfolding and aggregation into amyloid fibrils is an important strategy for therapeutic development. For example, Tafamidis is a small molecule stabilizer of the TTR protein that binds to the TTR protein and prevents it from misfolding and aggregating into amyloid fibrils.

Clear Amyloid Deposits

Clearing existing amyloid deposits in affected organs is another therapeutic strategy. Several monoclonal antibodies currently under investigation, such as birtimab, NEOD001, and daratumumab, are designed to recognize and clear amyloid deposits and modulate immune responses.

Our Services

Drawing upon our deep expertise in biotechnology and extensive experience in the industry, our company offers all-encompassing solutions for diagnostic and therapeutic research dedicated to amyloidosis.

Xenograft Models
Xenograft models involve the transplantation of human tissue or cells into immunodeficient animals. These models are particularly useful for studying localized forms of amyloidosis, in which deposition of amyloid fibrils occurs in specific organs or tissues.
Genetically Engineered Models
Our company is dedicated to the development of genetically engineered models for amyloidosis research. Our scientists have successfully integrated mutant human genes associated with amyloidosis into the mouse genome, effectively replicating the key characteristics of human amyloidosis. These transgenic models play a crucial role in assessing disease progression and evaluating the efficacy of therapeutic interventions.
Optional Models
  • IL-6 Transgenic Model
  • ApoA2c Transgenic Model
  • PrPsc Transgenic Model
  • V30M TTR Transgenic Model
  • L55P TTR Transgenic Model
  • T119M TTR Transgenic Model
  • I84S TTR Transgenic Model
  • SAP Knockout Model
Optional Species Mice, Rats, Nematodes, Drosophila, Non-Human Primates (Monkeys), Others

No matter what research stage you are at, we can provide you with corresponding research services. If you are interested in our services, please feel free to contact us for more details and quotation information for related services.


  • Ikura, Hidehiko, et al. "Molecular mechanism of pathogenesis and treatment strategies for AL amyloidosis." International journal of molecular sciences 23.11 (2022): 6336.
  • Picken, Maria M. "The pathology of amyloidosis in classification: a review." Acta haematologica 143.4 (2020): 322-334.

All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.

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