Recombinant Human Prealbumin protein
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Recombinant Human Prealbumin protein is a Human Full Length protein, in the 21 to 147 aa range, expressed in HEK 293 cells, with >95%, < 0.1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
PALB, TTR, Transthyretin, ATTR, Prealbumin, TBPA
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Lyophilized
Additional notes
ab152031 was determined to be >95% pure by SEC-HPLC and reducing SDS-PAGE.
General info
Function
Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Sequence similarities
Belongs to the transthyretin family.
Post-translational modifications
Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYLD1 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway.. Sulfonation of the reactive cysteine Cys-30 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation.
Target data
Product promise
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