Immunogen
Recombinant protein corresponding to the Human wild type Transthyretin. GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEH AEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE The epitope has been mapped to residue 56-61
Host
Mouse
Clonality
Monoclonal
Subclass/Isotype
IgG1
Purity
Affinity Purified
Format
Lyophilized
Quantity
100 μg
Reconstitution
Add 100 ul PBS to reconstitute to 1 mg/ml
Storage
Store lyophilized/reconstituted at 4°C. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
Tested applications
The antibody performs well in both ELISA, IHC and Western blot. Dry milk dissolved in TBS containing 0.3% Tween-20 provides a good blocking and incubation solution. Washing can preferably be performed using TBS containing 0.3% tween-20.
Recommended dilution
1:1000 (ELISA), 1:1000 (Western Blot) 1:500 (IHC)
Expected | apparent MW
155 kDa
Confirmed Reactivity
Human Transthyretin Amyloids only
Predicted Reactivity
No confirmed exceptions from predicted reactivity are currently known.
Not reactive in
Application Examples
Western analysis Membrane: PVDF Blocking buffer: 1% dry milk in TBS, 0.3% Tween 20 Antibody dilution : 1:1000 Secondary antibody: anti-mouse (HRP) Detection: Enhanced Chemoluminescence (pico) 150s
Additional information
Specifically reactive to the amyloid form of human Transthyretin. Epitope mapped to residue 56-61 which remains buried within the native fold of transthyretin but becomes exposed within its amyloid form. It has been suggested that that two distinct mechanisms of TTR-amyloidosis exists. The first, most common seen in wild type TTR Amyloidosis, consists of the full length TTR. Whereas the other type of amyloidosis mainly consists of the C-terminal region of the protein and is more common in mutant versions of TTR. Mouse IgG1 Anti-Transthyretin 56-61 (Amyloid Specific) epitope is located at the C-terminal strand of cleaved TTR and is suitable to detect amyloid formation derived from the C-terminal.
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