Transthyretin/TTR Protein, Human (HEK293, Fc-Myc)

Transthyretin (TTR) belongs to the serum transporter family and is a plasma transporter of T₄ and retinol. Transthyretin inhibits Aβ_1-42 fibrillization and is a potential target for amyloidosis and Alzheimer's disease. Transthyretin mutations (such as V30M) can destabilize the tetramer and promote the formation of amyloid fibrils in monomers, causing hereditary amyloidosis transthyretin (ATTRv). Transthyretin/TTR Protein, Human (HEK293, Fc-Myc) is a recombinant transthyretin/TTR protein expressed in HEK293 with C-hFc and C-Myc tag.

1. Protein characteristics of Transthyretin/TTR
Transthyretin (TTR) is a homotetramer linked by disulfide bonds, containing a conserved β-folded structure and two thyroxine (T₄) binding sites. Transthyretin/TTR needs to be cleaved by the signal peptide to form a mature protein, and the stability of the tetramer is maintained by T₄ binding^[1]. Transthyretin/TTR belongs to the serum transport protein family and is a plasma transporter of T₄ and retinol. Transthyretin/TTR forms a complex with retinol binding protein to mediate vitamin A transport and maintain the homeostasis of thyroid hormone and vitamin A^[2]. Mutations (such as V30M and L55P) can destroy the stability of Transthyretin/TTR tetramers, causing monomers to dissociate and self-assemble into β-sheet fibers, which are deposited in nerve, heart and other tissues to cause hereditary transthyretin amyloidosis (ATTRv). Non-fibrillar oligomers cause cytotoxicity through calcium influx and endoplasmic reticulum stress^[1].
Transthyretin/TTR binds to Aβ_1-42, inhibits its fibrillation through the T₄ binding pocket, and delays Alzheimer's disease-related pathology^[2]. Or Transthyretin/TTR and endogenous factors such as glycosaminoglycans synergistically promote amyloid deposition^[1].
2. Applications of Transthyretin/TTR
Transthyretin/TTR can be used to study the pathological mechanism of the amyloidosis disease ATTRv. For example, mutant (e.g., L55P) transgenic mice are constructed for drug screening, and Transthyretin/TTR stabilizers such as Diflunisal are studied, which delays amyloid fibril formation by stabilizing Transthyretin/TTR tetramers^[3]; meanwhile, the stabilizer Tafamidis has been shown to be useful for inhibiting ATTRv neuropathy^[1]. Transthyretin/TTRR targets Aβ aggregation and is a potential target for Alzheimer's disease^[2].

Measured by its binding ability in a functional ELISA. Immobilized RBP4 at 5 μg/mL can bind human TTR, the EC₅₀ of human TTR protein is 468.9-1769 ng/mL.

Human

HEK293

C-hFc;C-Myc

P02766 (G21-E147)

7276  [NCBI]

Full Length of Mature Protein

GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE

Approximately 47 kDa, based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, 6% trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Manganelli F, et al. Hereditary transthyretin amyloidosis overview. Neurol Sci. 2022 Dec;43(Suppl 2):595-604.  [Content Brief]

  [2]. Li X, et al. Mechanisms of transthyretin inhibition of β-amyloid aggregation in vitro. J Neurosci. 2013 Dec 11;33(50):19423-33.  [Content Brief]

  [3]. Tagoe CE, et al. In vivo stabilization of mutant human transthyretin in transgenic mice. Amyloid. 2007 Sep;14(3):227-36.  [Content Brief]