for Research Use Only
for Amyloidosis research
Transthyretin(TTR),recombinant
Wako Catalog No. 209-17301 (1 mg) : Wild-type
No. 206-17311 (1 mg) : Variant (V30M)
No. 203-17321 (1 mg) : Variant (L55P)
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Transthyretin (TTR) protein is a soluble nonglycosylated protein, which has 127-amino-acids, normally
circulates in plasma or cerebrospinal fluid. It is shown to be a 55,000-Da tetramer with four identical
subunits. TTR plays important physiological roles as a transporter of thyroxine and retinol-binding protein.
TTR is also known as one of the precursor proteins commonly found in amyloid deposits. Amyloidosis is
a disorder that causes dysfunction of the organs by deposition of fibrous proteins, amyloids, which are
insolubilized by protein denaturation and aggregation. Wild-type TTR deposition leads to senile amyloid
disease. On the other hand, familial amyloidosis, associated with one of over 100 TTR mutations typically
present earlier, are often more severe, with several variants exhibiting tissue-selective deposition and
pathology.
Clinical pictures depend on the kind of mutations. Traditionally-investigated V30M mutation,
a substitution of methionine (M) for valine (V) at position 30, causes symptoms such as sensorimotor
and autonomic neuropathies and when the symptoms progress, cardiomyopathy and nephropathy are
developed. The L55P mutation, a substitution of proline (P) for leucine (L) at position 55, causes
extremely severe amyloidosis.
Amyloid fiber
L55
V30
TTR
L55P mutation
Self-association
V30M mutation
for other product information, please visit the Wako Online Catalog http://www.e-reagent.com
Amino-Acid Sequences
Wild-type (Wako Cat. No. 209-17301)
MRGSHHHHHHGS+GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELH
6 X His-tag
GLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIA ALLSPYSYSTTAVVTNPKE
V 30 M (Wako Cat. No. 206-17311)
MRGSHHHHHHGS+GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELH
6 X His-tag
GLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIA ALLSPYSYSTTAVVTNPKE
L 55 P (Wako Cat. No. 203-17321)
MRGSHHHHHHGS+GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGEPH
6 X His-tag
GLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIA ALLSPYSYSTTAVVTNPKE
Strage Condition
Keep at -20ºC
References
1 )
2 )
3 )
Hamilton, J. A. and Benson, M. D. : "Transthyretin : a review from a structural perspective", Cell. Mol. Life Sci.,
58, 1491-1521 (2001).
Sekijima, Y., Wiseman, R. L., Matteson, J., Hammarström, P., Miller, S.R., Sawkar, A. R., Balch, W. E. and Kelly,
J. W. : "The Biological and Chemical Basis for Tissue-Selective Amyloid Disease" Cell, 121, 73 (2005).
Sekijima, Y., Yoshida, K., Tokuda, T. and Ikeda, S. : (Mar. 2006) "Transthyretin Amyloidosis" , In : Gene Reviews
at Gene Tests Medical Genetics Information Resource (database online). Copyright, Univ. of Washington, Seattle
1993-2009. Available at http://www.genetest.org/Accessed Jan. 21, 2009
Description
Grade
Wako Cat. No.
(Pkg. Size)
Note
Transthyretin (Wild-type)
Transthyretin Variant (V 30M)
Transthyretin Variant (L 55P)
Human, recombinant, Lyophilized
[Source : E. coli expressed human transthyretin]
Human, recombinant, Lyophilized
[Source : E. coli expressed human transthyretin variant (V 30M)]
Human, recombinant, Lyophilized
[Source : E. coli expressed human transthyretin variant (L 55P)]
for Cellbiology
for Cellbiology
for Cellbiology
209-17301
206-17311
203-17321
(1 mg)
(1 mg)
(1 mg)
• MW : 15,100
(6 X Histidine-
tagged monomer)
• Buffer :
20 mmol/L
Ammonium bicarbonate
• Keep at -20ºC