After search, choose a molecule or a kind of categories listed in the left to narrow down your filter. If you have any problems, please contact us!
Text Size:AAA

Human Prealbumin / Transthyretin / TTR / PALB Protein (His Tag)

DatasheetSpecific ReferencesReviewsRelated ProductsProtocols
Human TTR Protein Product Information
Synonym:HsT2651, PALB, TBPA
Protein Construction:A DNA sequence encoding the human TTR (NP_000362.1) (Met 1-Glu 147) with a C-terminal polyhistidine tag was expressed.
Expressed Host:Human Cells
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Human TTR Protein QC Testing
Purity:> 97 % as determined by SDS-PAGE
Bio-Activity:Measured by its binding ability in a functional ELISA.
Immobilized recombinant human TTR-His (Cat:12091-H08H)at 10 μg/ml (100 μl/well) can bind recombinant Canine RBP4-Fc (Cat:70006-D02H) with a linear range of 0.3-10.0 μg/ml.
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Gly 21
Molecule Mass:The secreted recombinant human TTR comprises 138 amino acids with a predicted molecular mass of 15.2 kDa. As a result of glycosylation, the apparent molecular mass of rhTTR is approximately 19 and 38 kDa in SDS-PAGE under reducing conditions, corresponding to the monomer and dimer respectively.
Formulation:Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Human TTR Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Human TTR Protein SDS-PAGE
Human Prealbumin / Transthyretin / TTR / PALB Protein (His Tag) SDS-PAGE
Other TTR Recombinant Protein Products
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.

Human Prealbumin/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.
  • Product nameProduct name
    Size / Price
    Catalog: 12091-H08H-50
    List Price:   (Save )
    Price:      [How to order]
    AvailabilityIn StockShipping instructions