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AB92931

Recombinant Human Prealbumin protein (Tag Free)

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Recombinant Human Prealbumin protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

PALB, TTR, Transthyretin, ATTR, Prealbumin, TBPA

1 Images
SDS-PAGE - Recombinant Human Prealbumin protein (Tag Free) (AB92931)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Prealbumin protein (Tag Free) (AB92931)

15% SDS-PAGE analysis of 3μg ab92931

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P02766

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS, 10% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P02766","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Prealbumin also known as transthyretin is a protein with a molecular mass of approximately 55 kDa. The liver primarily synthesizes prealbumin and it is present in the bloodstream. Functionally prealbumin transports thyroxine and retinol-binding protein-retinol complex facilitating the distribution of these molecules to target tissues. As such it plays an integral role in maintaining retinol and thyroid hormone homeostasis.
Biological function summary

Prealbumin interacts with retinol-binding protein to form a complex essential for vitamin A transportation. This complex prevents renal filtration of retinol-binding protein thereby conserving vitamin A in circulation. The protein's role extends beyond transport as it influences neurophysiological processes due to its ability to bind thyroid hormones and affect gene expression related to metabolism. Prealbumin is primarily a part of the thyroxine-transferring complex reinforcing its critical position in hormonal and vitamin dynamics.

Pathways

Prealbumin's role in the thyroxine-binding globulin pathway highlights its importance in the endocrine system. Another pathway where prealbumin contributes significantly is the vitamin A metabolic pathway. In these pathways prealbumin maintains functional relationships with proteins like retinol-binding protein and thyroxine-binding globulin which jointly modulate thyroid hormone transport and vitamin A dynamics across cellular membranes.

Prealbumin directly associates with familial amyloid polyneuropathy and malnutrition. Familial amyloid polyneuropathy involves the deposition of prealbumin-derived amyloid fibrils in peripheral nerves impacting neuron function. In malnutrition decreased prealbumin levels serve as a biomarker reflecting poor nutritional status. Clinically prealbumin's relation to retinol-binding protein and thyroid hormone levels facilitates its use in diagnosing and monitoring these conditions.

Specifications

Form

Liquid

Additional notes

Purified using conventional chromatography.

General info

Function

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.

Sequence similarities

Belongs to the transthyretin family.

Post-translational modifications

Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYLD1 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway.. Sulfonation of the reactive cysteine Cys-30 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation.

Product protocols

Target data

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
See full target information TTR

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