Description

  • Product name

    Native Human Prealbumin protein
    See all Prealbumin proteins and peptides
  • Purity

    > 95 % SDS-PAGE.

  • Expression system

    Native
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Native
    • Species

      Human

Specifications

Our Abpromise guarantee covers the use of ab90922 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

  • Form

    Lyophilised
  • Additional notes

    Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20ºC.

    pH: 7.50
    Constituents: 0.82% Sodium phosphate, 0.87% Sodium chloride

  • Reconstitution
    Please reconstitute with deionized water to the pre-lyophilization volume (lot specific).

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
  • Function

    Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
  • Tissue specificity

    Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver.
  • Involvement in disease

    Defects 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 similarities

    Belongs to the transthyretin family.
  • Domain

    Each 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 localization

    Secreted. Cytoplasm.
  • Information by UniProt

References

ab90922 has not yet been referenced specifically in any publications.

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