Anti-Beta (β)-Amyloid antibody

Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. In disease state oligomerization, extensive amyloid oligomerization creates plaques in neural tissue that correlates with Alzheimer’s symptomology.

Fibrils prepared from human islet amyloid polypeptide.

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.

This Anti-Amyloid Fibrils LOC Antibody is validated for use in IP, IC, IH, ELISA, WB, DB for the detection of Amyloid Fibrils LOC.

This antibody recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not monomers, prefibrillar oligomers or natively folded proteins.

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. After thawing, store at 4°C in 0.02% sodium azide.

Evaluated by Dot Blot in monomers, prefibril oligos, and fibrils.

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.

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