TTR Specific Neutra™ Antibody Products
Product listTransthyretin (TTR), also known as prealbumin, is a transport protein of thyroid hormone and retinol. TTR is predominantly produced by the liver and released into the bloodstream. It exists as well in the brain and eyes. TTR is composed of four identical subunits, each containing 127 amino acids, and is responsible for the stable and efficient delivery of these essential compounds throughout the body. The expression and secretion of TTR are tightly regulated, ensuring the proper distribution and maintenance of thyroid hormones and vitamin A homeostasis, which are vital for various physiological processes.
Its Gene ID: 7276, UniProtKB ID: P02766, and OMIM ID: 176300.
Functions of TTR
TTR plays vital roles in the transport of thyroxine (T4) and retinol, as well as in proteolytic activity, contributing to metabolism and various physiological processes in the body. Firstly, it acts as a carrier protein for T4, facilitating its transport in the bloodstream and ensuring its delivery to target tissues for metabolism and biological activity. Additionally, TTR also binds to retinol (vitamin A) and transports it in the blood, contributing to the systemic distribution of this essential nutrient. Moreover, TTR exhibits proteolytic activity on several substrates. This proteolytic function of TTR helps to maintain protein homeostasis and avoid the accumulation of aberrant protein aggregates that can lead to diseases like amyloidosis.
Role of TTR in Diseases
TTR is implicated in several diseases, notably in the context of amyloidosis. Mutations in the TTR gene can lead to the production of variant TTR proteins that misfold and aggregate, forming amyloid fibrils. These fibrils deposit in various tissues, causing systemic amyloidosis, which can manifest as neurological dysfunction, cardiomyopathy, or peripheral neuropathy. Additionally, decreased levels of TTR have been associated with malnutrition, chronic inflammation, and certain types of cancer. Conversely, elevated TTR levels have been observed in conditions like familial amyloidotic polyneuropathy.
Fig.1 Overview of the development of hereditary transthyretin cardiac amyloidosis.1
Antibodies Targeting TTR
Monoclonal antibodies (mAbs) targeting TTR have been widely studied in TTR amyloidosis and tested in various clinical trials with promising results. These antibodies can selectively bind to and remove amyloid deposits, preventing the deposition of TTR amyloid, promoting the clearance of TTR amyloid, and diagnosing TTR amyloidosis. For instance, one mAb targeting aggregated TTR can bind to transthyretin amyloidosis (ATTR) fibrils and cause considerable clearance of ATTR aggregates via antibody-dependent phagocytosis. Preclinical studies have also demonstrated the role of anti-TTR mAb in reversing cardiac dysfunction in patients with transthyretin amyloid cardiomyopathy. Besides, in the familial amyloidotic polyneuropathy model rats, one anti-TTR mAb shows effective therapeutic effects by inhibiting TTR accumulation and exhibiting non-fibrillar ATTR deposits in the gastrointestinal system.
Fig.2 Proposed model for the inhibition of TTR fibrillogenesis by the anti-TTR antibody.2
Creative Biolabs offers more than thirty different anti-TTR antibody products to meet your various research needs. These antibodies are recombinantly expressed and could be used in eight applications.
REFERENCES
- Williams, Marcus AC, et al. "Current and potential therapeutic strategies for transthyretin cardiac amyloidosis." Frontiers in Drug Discovery 2 (2022): 1015545. Distributed under Open Access license CC BY 4.0, without modification.
- Galant, Natalie J., et al. "Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses." Scientific reports 6.1 (2016): 25080. Distributed under Open Access license CC BY 4.0, without modification.
