The TTR Antibody (PAC030874) is a polyclonal antibody designed for research involving Transthyretin (TTR), a protein primarily produced by the liver and involved in the transport of thyroid hormones and vitamin A. The antibody, raised in rabbits, is highly reactive with human samples and is validated for use in various applications such as Western blot and immunohistochemistry.Transthyretin is a key protein in the regulation of thyroid hormones and vitamin A, making it a crucial target for research in endocrinology, metabolism, and neurological disorders.
Dysregulation of TTR has been implicated in diseases such as familial amyloid polyneuropathy and senile systemic amyloidosis, highlighting the importance of studying its expression and function.Through its specificity in binding to Transthyretin, the TTR Antibody enables detection and analysis of TTR levels in different tissues and cell types. This makes it an invaluable tool for investigating the role of Transthyretin in various physiological and pathological conditions, aiding in the advancement of research and potential therapeutic interventions.
Antibody Name:
Ttr Antibody (PACO30874)
Antibody SKU:
PACO30874
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, IHC
Recommended Dilutions:
ELISA:1:2000-1:10000, IHC:1:20-1:200
Species Reactivity:
Mouse
Immunogen:
Recombinant Mouse Transthyretin protein (23-147AA)
Immunohistochemistry of paraffin-embedded human pancreatic tissue using PACO30874 at dilution of 1:100.
Synonyms:
Transthyretin (Prealbumin), Ttr
UniProt Protein Function:
TTR: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR). A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. Defects in TTR are a cause of hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE). It is a condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities. Defects in TTR are a cause of carpal tunnel syndrome type 1 (CTS1). It is a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. Belongs to the transthyretin family.
UniProt Protein Details:
Protein type:Secreted, signal peptide; Secreted
Cellular Component: extracellular region; extracellular space; protein complex
Molecular Function:hormone activity; hormone binding; identical protein binding; protein binding; protein heterodimerization activity
Biological Process: retinol metabolic process; transport
NCBI Summary:
This gene encodes a carrier protein responsible for the transport of thyroid hormones and retinol. The protein consists of a tetramer of identical subunits. Due to increased stability of the tetramer form of this encoded protein in mouse, compared to the human protein, this gene product has a reduced tendency to form amyloid fibrils. In humans, this protein binds beta-amyloid preventing its aggregation and providing a neuroprotective role in Alzheimer's disease. [provided by RefSeq, Mar 2010]
