Anti-Prealbumin antibody (Biotin) (ab48323)
- Product nameAnti-Prealbumin antibody (Biotin)See all Prealbumin primary antibodies ...
- DescriptionRabbit polyclonal to Prealbumin (Biotin)
- SpecificityThis antibody is specific for Prealbumin.
- Tested applicationsWB, RIA, IP more details
- Species reactivityReacts with: Human
Full length native Prealbumin (purified from plasma) (Human).
- Storage instructionsStore at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
- Storage bufferPreservative: 0.01% Thimerosal (merthiolate)
Constituents: 50% Glycerol, PBS, pH 7.5
- Concentration information loading...
- PurityProtein G purified
- Clonality Polyclonal
- Research Areas
Our Abpromise guarantee covers the use of ab48323 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||WB: Use at an assay dependent dilution. Predicted molecular weight: 16 kDa.|
|RIA||RIA: Use at an assay dependent dilution.|
|IP||IP: Use at an assay dependent dilution.|
- FunctionThyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
- Tissue specificityDetected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver.
- Involvement in diseaseDefects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR) [MIM:105210]. 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) [MIM:145680]. 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) [MIM:115430]. 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.
- Sequence similaritiesBelongs to the transthyretin family.
- DomainEach monomer has two 4-stranded beta sheets and the shape of a prolate ellipsoid. Antiparallel beta-sheet interactions link monomers into dimers. A short loop from each monomer forms the main dimer-dimer interaction. These two pairs of loops separate the opposed, convex beta-sheets of the dimers to form an internal channel.
- Cellular localizationSecreted. Cytoplasm.
- Amyloid polyneuropathy antibody
- Amyloidosis I antibody
- ATTR antibody
- Carpal tunnel syndrome 1 antibody
- CTS antibody
- CTS1 antibody
- Dysprealbuminemic euthyroidal hyperthyroxinemia antibody
- Dystransthyretinemic hyperthyroxinemia antibody
- HsT2651 antibody
- PALB antibody
- Prealbumin amyloidosis type I antibody
- Prealbumin antibody
- Senile systemic amyloidosis antibody
- TBPA antibody
- Thyroxine binding prealbumin antibody
- Transthyretin antibody
- TTHY_HUMAN antibody
- TTR antibody
- TTR protein antibody
References for Anti-Prealbumin antibody (Biotin) (ab48323)
ab48323 has not yet been referenced specifically in any publications.