Recombinant Human Prealbumin protein (ab88120)

Overview

Description

  • NatureRecombinant
  • SourceSaccharomyces cerevisiae
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceMASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAV HVFRKAAD DTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSY WKALGISPFHEHAEVVFT ANDSGPRRYTIAALLSPYSYSTTAVVTNPK E

Specifications

Our Abpromise guarantee covers the use of ab88120 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Purity> 90 % SDS-PAGE.
    ab88120 was purified by affinity chromatography.
  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 30% Glycerol, 0.5% Triton-X-100, 50mM HEPES, 30mM Glutathione, 100mM Sodium chloride, 1mM DTT, pH 7.5

General Info

  • Alternative names
    • Amyloid polyneuropathy
    • Amyloidosis I
    • ATTR
    • Carpal tunnel syndrome 1
    • CTS
    • CTS1
    • Dysprealbuminemic euthyroidal hyperthyroxinemia
    • Dystransthyretinemic hyperthyroxinemia
    • Epididymis luminal protein 111
    • HEL111
    • HsT2651
    • PALB
    • Prealbumin
    • Prealbumin amyloidosis type I
    • Prealbumin Thyroxine-binding
    • Senile systemic amyloidosis
    • TBPA
    • Thyroxine binding prealbumin
    • Transthyretin
    • TTHY_HUMAN
    • TTR
    • TTR protein
    see all
  • 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.
  • Information by UniProt

References for Recombinant Human Prealbumin protein (ab88120)

ab88120 has not yet been referenced specifically in any publications.

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