- SynonymTransthyretin,TTR,Prealbumin,TBPA,ATTR,PALB,CTS,CTS1,HsT2651
- SourceHuman Transthyretin, His Tag (TTR-H5223) is expressed from human 293 cells (HEK293). It contains AA Gly 21 - Glu 147 (Accession # NP_000362).Predicted N-terminus: Gly 21Request for sequence
- Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 14.9 kDa. The protein migrates as 19 kDa and 37 kDa under reducing (R) condition (SDS-PAGE) due to the monomer and dimer respectively.
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>95% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human Transthyretin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
- BackgroundTransthyretin (TTR) is also known as Prealbumin, ATTR, TBPA, PALB, which belongs to the transthyretin family. Transthyretin / TTR is a serum and cerebrospinal fluid carrier of the thyroid hormone thyroxine (T4) and retinol-binding protein bound to retinol. In cerebrospinal fluid TTR is the primary carrier of T4. TTR also acts as a carrier of retinol (vitamin A) through its association with retinol-binding protein (RBP) in the blood and the CSF. Less than 1% of TTR"s T4 binding sites are occupied in blood. TTR misfolding and aggregation is known to be associated with the amyloid diseases.
- References
- (1)Getz R.K., et al., 1999, Exp. Eye Res. 68:629-636.
- (2)Herbert J., et al., 1986, Neurology 36:900-911.
- (3)Mita S., et al., 1984, Biochem. Biophys. Res. Commun. 124:558-564.
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