• Product name

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

    > 95 % SDS-PAGE.

  • Expression system

  • Protein length

    Full length protein
  • Animal free

  • Nature

    • Species



Our Abpromise guarantee covers the use of ab77905 in the following tested applications.

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

  • Applications


    Western blot

  • Form

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

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

  • Reconstitution
    Reconsitute with deionized water

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
    • 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



ab77905 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

1-2 of 2 Abreviews or Q&A

Western blot
We use this product for Western and dot blot assays. We study prealbumin aggregation and its relevance to human diseases. Because of this focus, we use this protein both for its native form and to make aggregates of the protein using standard methods (low pH, heat at 37 C). In both forms, this protein works well for dot blot and Western assays. This protein will not aggregate as readily some of the more well-described amyloidogenic mutant forms, as expected.

Overall, we've seen good lot to lot consistency with this product. Using native PAGE gels, we see almost exclusively tetramer, while with heating and SDS, we see monomer and dimer. The only real issue we've encountered occurs when we attempt to load large amounts of the protein (ug range), which is necessary to visualize the aggregated form of the protein. When we do so, we see a band above the tetramer in our native PAGE gels that has a weight of about 86 kDa (shown in attached image). Abcam's technical support had this to say about the band (note that the product is plasma purified, NOT recombinant):

"Thus, you may be detecting a form of TTR that is not normally seen. Another possibility is that due to the role of TTR, a small portion of the molecules that are contained in the purified product may be complexed with Retinol binding protein. This was not detected in the QC of the final product but given the large amount of protein that is being run on the Western Blot, it is possible that it could show up."

Overall, then, we've been happy with the product and found it useful as a negative (native) and positive (aggregated) control for our assays looking for aggregated TTR in biological fluid.

Abcam user community

Verified customer

Submitted Sep 05 2014


Prealbumin is a tetramer under native conditions. It has a molecular weight of ~ 56,000 Da which consists of 4 subunits of ~ 14,000 Da each. When the lab runs native electrophoresis on this protein, we also only see the tetramer, and the monomer is only seen under reduced and denatured conditions.

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