Recombinant Human Prealbumin protein (Tagged) (ab267993)
Key features and details
- Expression system: Mammalian
- Purity: > 85% SDS-PAGE
- Tags: Fc tag C-Terminus
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Human Prealbumin protein (Tagged)
See all Prealbumin proteins and peptides -
Purity
> 85 % SDS-PAGE. -
Expression system
Mammalian -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTS ESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDS GPRRYTIAALLSPYSYSTTAVVTNPKE -
Predicted molecular weight
15 kDa -
Amino acids
21 to 147 -
Tags
Fc tag C-Terminus -
Additional sequence information
Mature chain with C-terminal FC-Myc-tag.
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab267993 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 7.2
Constituents: PBS, 6% Trehalose
Lyophilized from.
General Info
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Alternative names
- Amyloid polyneuropathy
- Amyloidosis I
- ATTR
see all -
Function
Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. -
Tissue specificity
Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver. -
Involvement in disease
Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR) [MIM:105210]. A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor.
Defects in TTR are a cause of hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE) [MIM:145680]. It is a condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities.
Defects in TTR are a cause of carpal tunnel syndrome type 1 (CTS1) [MIM:115430]. It is a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. -
Sequence similarities
Belongs to the transthyretin family. -
Domain
Each monomer 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. -
Cellular localization
Secreted. Cytoplasm. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab267993 has not yet been referenced specifically in any publications.