Transthyretin Proteins, Antibodies, cDNA Clones Research Reagents

TTR (Transthyretin) is a protein coding gene located on human chromosome 18q12.1. TTR is also known as CTS, ATTR, CTS1, PALB, TBPA, HEL111 and HsT2651. The human TTR gene encodes a 15887 Da protein containing 147 amino acids. The TTR protein is restrictedly expressed toward liver. Among its related pathways are Signaling by GPCR and Degradation of the extracellular matrix. TTR is related to identical protein binding and hormone activity. URAD is an important paralog of TTR gene. TTR is associated with some diseases, including Amyloidosis, Hereditary, Transthyretin-Related and Hyperthyroxinemia, Dystransthyretinemic.

Transthyretin Protein (3)

    Transthyretin Antibody (5)

      Transthyretin cDNA Clone (40)

      NM_000371
      NM_013697.5
      AF479660.1
      XM_537290.3

      In cloning vector

      Transthyretin Lysate (3)

        Transthyretin Background

        Prealbumin/Transthyretin, also known as ATTR, Prealbumin, TTR and PALB, is a secreted and cytoplasm protein that belongs to the Prealbumin / Transthyretin family. Prealbumin / Transthyretin is detected in serum and cerebrospinal fluid (at protein level). It is highly expressed in choroid plexus epithelial cells. It is also detected in retina pigment epithelium and liver. Each monomer of Prealbumin / Transthyretin 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. Prealbumin/Transthyretin is a carrier protein. It transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Defects in Prealbumin / Transthyretin are the cause of amyloidosis type 1 (AMYL1) which is a hereditary generalized amyloidosis due to Prealbumin / Transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, carpal tunnel syndrome, etc.

        Transthyretin References

        • Westermark P, et al. (1990) Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A. 87(7): 2843-5.
        • Colon W, et al. (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry. 31(36): 8654-60.
        • Hammarstrm P, et al. (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science. 299(5607): 713-6.

        Note: Flag® is a registered trademark of Sigma Aldrich Biotechnology LP. It is used here for informational purposes only.