Description
Key facts
Purity:>90% SDS-PAGE,
Expression system:Mammalian,
Tags:His tag N-Terminus,
Applications:SDS-PAGE, Mass SpecSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q8HXW1,
Animal free:No,
Carrier free:No,
Species:Cynomolgus monkey,
Storage buffer:pH: 7.2 - 7.4Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Prealbumin also known as transthyretin is a protein with a molecular mass of approximately 55 kDa. The liver primarily synthesizes prealbumin and it is present in the bloodstream. Functionally prealbumin transports thyroxine and retinol-binding protein-retinol complex facilitating the distribution of these molecules to target tissues. As such it plays an integral role in maintaining retinol and thyroid hormone homeostasis.
Biological function summary
Prealbumin interacts with retinol-binding protein to form a complex essential for vitamin A transportation. This complex prevents renal filtration of retinol-binding protein thereby conserving vitamin A in circulation. The protein's role extends beyond transport as it influences neurophysiological processes due to its ability to bind thyroid hormones and affect gene expression related to metabolism. Prealbumin is primarily a part of the thyroxine-transferring complex reinforcing its critical position in hormonal and vitamin dynamics.
Pathways
Prealbumin's role in the thyroxine-binding globulin pathway highlights its importance in the endocrine system. Another pathway where prealbumin contributes significantly is the vitamin A metabolic pathway. In these pathways prealbumin maintains functional relationships with proteins like retinol-binding protein and thyroxine-binding globulin which jointly modulate thyroid hormone transport and vitamin A dynamics across cellular membranes.
Prealbumin directly associates with familial amyloid polyneuropathy and malnutrition. Familial amyloid polyneuropathy involves the deposition of prealbumin-derived amyloid fibrils in peripheral nerves impacting neuron function. In malnutrition decreased prealbumin levels serve as a biomarker reflecting poor nutritional status. Clinically prealbumin's relation to retinol-binding protein and thyroid hormone levels facilitates its use in diagnosing and monitoring these conditions.
