TTR Protein

€141,000.00
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SKU:
SPR-465E
Availability:
Next week
Shipping:
Calculated at Checkout
Size:
5x100 µg
Species:
Human
Specificity:
15.887 kDa
Conjugate:
No Tag
Storage Temperature:
-80ºC
Purity:
>95%
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TTR Protein is available at Gentaur for Next week delivery.

Description:  Human Recombinant Transthyretin Y78F Variant Protein Filaments

Alternative Name(s):  Amyloid polyneuropathy Protein, Amyloidosis I Protein, ATTR Protein, Carpal tunnel syndrome 1 Protein, CTS Protein, CTS1 Protein, HEL111 Protein, HsT2651 Protein, PALB Protein, Prealbumin Protein, Prealbumin amyloidosis type I Protein, Prealbumin Thyroxine-binding Protein, TBPA Protein, Thyroxine binding prealbumin Protein, Transthyretin Protein, TTHY_HUMAN Protein,TTR Protein

Research Area(s):  Alzheimer's Disease | Axon Markers | Cell Markers | Cell Signaling | Cytoskeleton | Microtubules | MT Associated Proteins | Neurodegeneration | Neuron Markers | Neuroscience | Tangles & Tau

Nature:  Recombinant

Accession Number: NP_000362.1

Gene ID:  7276

Swiss-Prot:  P02766 

Applications Species:  WB | SDS-PAGE | In vivo assay | In vitro assay 

Biological Activity: 

Expression System: E. coli

Protein Length:  Full length

Amino Acid Sequence:

Purification:  Ion-exchange Purified

Storage Buffer:  PBS pH 7.4

Concentration:  Lot/batch specific. See included datasheet.

Shipping Temperature: Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.

Other relevant information: For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or on the product datasheet for further information..

Certificate of Analysis: Certified >95% pure using SDS-PAGE analysis. 

Cellular Localization:  Cytoplasm | Extracellular exosome | Extracellular Region | Lysosome

Scientific Background:  Transthyretin is a transport protein in the serum and cerebospinal fluid that carried the thyroid hormone Thyroxine and retinol-binding protein bound to retinol. TTR misfolding and aggregation is known to be associated with the amyloiddiseases SSA, FAP and FAC (1-5). TTR is also thought to have beneficial side effects, such as binding to beta-amyloid protein, preventing beta-amyloid from accumulating into the plaques associated with Alzheimer's Disease (6). The mutant variant Y78F indicates a destabilization of the contacts between the alpha-helix and AB loop and the body of the molecule, potentially leading to applications in immne therapy for FAP (7).

References: 1. Zeldenrust S.R., Benson M.D. (2010). Wiley. pp. 795–815. 2. Westermark P., Sletten K., Johansson B., Cornwell G.G. (1990). Proc. Natl. Acad. Sci. U.S.A. 87(7): 2843–5. 3. Andrade C. (1952). Brain. 75(3): 408–27. 4. Coelho T. (1996). Curr. Opin. Neurol. 9(5): 355–9. 5. Jacobson D.R, et. al. (1997). N. Engl. J. Med. 336(7): 466–73. 6. Li X. (2011). Mol Neurodegener. 6(1):79. 7. Terazaki H.,m et al. (2006) Lab Invest. 86(1): 23-31.

Field of Use:  Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

PubMed ID: 

Published Application: 

Published Species Reactivity: 

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