Transthyretin 39-44, amyloid specific (mouse monoclonal)

Product no: AS16 3112

AS16 3112   | Clonality: monoclonal  |  Host: Mouse  |  Reactivity: Human

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  • Product Info
  • Sub class: IgG
    Immunogen: Full length variant TTR,
    Host: Mouse
    Clonality: Monoclonal
    Purity: Affinity purified in PBS pH 7.4.
    Format: Lyophilized
    Quantity: 100 µg
    Reconstitution: For reconstitution add 100 µl of sterile water
    Storage: For short time storage please add sodium azide and srote at +4°C.For long time storage store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. 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:

    5 μg/ml (ELISA), 2 µg/ml (WB), 5 µg/ml (IHC)

  • Reactivity
  • Confirmed reactivity: Human
    Not reactive in: No confirmed exceptions from predicted reactivity are currently known
  • Application Examples



  • Background
  • Background:

    Transthyretin is a carrier protein in plasma of the thyroid hormone. This protein forms a complex with retinol-binding protein and it has the capability of forming amyloid fibrils. 25% of individuals older than 80 years are affected by senile systemic amyloidosis and most cases of TTR-associated amyloidosis are linked to point mutations. A substitution of valine for methionine at position 30 of the 127-aa-long polypeptide is one of the most common forms, leading to many symptoms in the peripheral nervous system, a familial amyloidosis with polyneuropathy.

    This monoclonal IgG1 antibody is amyloid specific for human Transthyretin. Detects the N-terminal fragment TTR-1-48 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
  • Protocols


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