Prealbumin / Transthyretin Protein & Antibody (TTR)

Prealbumin / Transthyretin Products

Prealbumin / Transthyretin Protein, Recombinant

Molecule	Species	Description	Cat. No
Prealbumin/Transthyretin	Human	Prealbumin/Transthyretin Protein, Recombinant	12091-H08H

Prealbumin / Transthyretin Antibogy

Molecule	Application	Description	Cat. No
Human GFRA1	WB, ELISA	GFRA1 Antibody, Rabbit MAb	12091-R003
Human GFRA1	WB, ELISA	Prealbumin / Transthyretin / TTR Antibody (Antigen Affinity Purified)	12091-RP02

Prealbumin / Transthyretin cDNA Clone

Molecule	Species	Description	Cat. No
Prealbumin/Transthyretin	Human	Homo sapiens Prealbumin/Transthyretin cDNA Clone	HG12091-G
Prealbumin/Transthyretin	Mouse	Mouse Prealbumin/Transthyretin cDNA Clone / ORF Clone	MG50958-G

Prealbumin / Transthyretin Alternative Names

Prealbumin, Transthyretin, TTR, ATTR, HsT2651, PALB, TBPA [Homo sapiens]

Prealbumin, Transthyretin, Ttr, AA408768, AI787086, D17860, MGC107649 [Mus musculus]

Prealbumin / Transthyretin Background

Prealbumin/Transthyretin, also known as ATTR, Prealbumin, TTR and PALB, is a secreted and cytoplasm protein which 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.

Prealbumin / Transthyretin Related Studies

1. 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.
2. Colon W, et al. (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry. 31(36): 8654-60.
3. Hammarström P, et al. (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science. 299(5607): 713-6.