Transthyretin 56-61, amyloid specific (mouse monoclonal)
AS16 3113 | clonality: monoclonal | host: mouse | reactivity: human

Data sheet | Product citations | Protocols | Add review |
Product Information
Immunogen
Recombinant protein corresponding to the Human wild type Transthyretin. GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELH
GLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYS
YSTTAVVTNPKE The epitope has been mapped to residue 56-61
GLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYS
YSTTAVVTNPKE The epitope has been mapped to residue 56-61
Host
Mouse
Clonality
Monoclonal
Subclass/isotype
IgG1
Purity
Affinity purified in PBS pH 7.4.
Format
Lyophilized
Quantity
100 ĩg
Reconstitution
Add 100 ĩl sterile water to reconstitute to 1 mg/ml
Storage
Store lyophilized/reconstituted at 4°C, Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Tested applications
ELISA (ELISA), Immunohistochemistry (IHC), Western blot (WB)
Recommended dilution
1:1000 (ELISA), 1:500 (IHC), 1:1000 (WB)
Expected | apparent MW
155
Reactivity
Confirmed reactivity
Human Transthyretin Amyloids
Not reactive in
No confirmed exceptions from predicted reactivity are currently known
Application examples
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.
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.
Background
Background
Transthyretin (TTR), formerly known as Prealbumin, is in vivo involved in the binding and transportation of the Thyroxin hormone and retinol-binding protein. Mutations in TTR are associated with familial amyloidotic polyneuropathy (FAP) which is a fatal disease characterized by amyloid depositions found in visceral organs including the heart, liver, and kidney. The wild type form of TTR is associated with a late onset amyloidosis denoted senile systemic amyloidosis, affecting around 10% of the population above 80 years of age with depositions mainly found in the heart.
Monoclonal IgG1 antibody. Amyloid specific for human Transthyretin. Detects the C-terminal fragment 49-127 frequently formed in vivo.
Monoclonal IgG1 antibody. Amyloid specific for human Transthyretin. Detects the C-terminal fragment 49-127 frequently formed in vivo.
Product citations
Selected references
Goldsteins et al. (1999). Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants. Proc Natl Acad Sci U S A. 1999 Mar 16; 96(6): 3108–3113
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