Product Name:
Amyloid Oligomers (A11)
Product Number:
ab-nn198-1
Target Full Name: Amyloid beta A4 protein
Target Alias: OC; Fibrils; Amyloid Oligomer aß; A11; Amyloid beta A4 protein; ABPP; APPI; Cerebral vascular amyloid peptide; PreA4; Protease nexin-II; APP; A4; AD
Product Type Specific: Amyloid protein pan-specific antibody
Antibody Code: NN198-1
Antibody Target Type: Pan-specific
Protein UniProt: P05067
Protein SigNET: Amyloid Oligomers (A11)
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Ig Isotype Clone: N/A
Antibody Immunogen Source: Synthetic molecular mimic of soluble oligomers
Production Method: Protein A purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Storage Buffer: Phosphate buffered saline, 50% glycerol, 0.09% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | Immunohistochemistry | ICC/Immunofluorescence | Immunoprecipitation | ELISA
Antibody Dilution Recommended: WB (1:1000), IP (1:1000); optimal dilutions for assays should be determined by the user.
Antibody Potency: Recognizes all types of amyloid oligomers. Appears to recognize a peptide backbone epitope that is common to amyloid oligomers, but is not found in native proteins, amyloidogenic monomer or mature amyloid fibrils.
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Rat | Mouse | Eukaryotes.
Antibody Positive Control: A 1:1000 dilution of SPC-506 was sufficient for detection of amyloid oligomers in 10 µg of mouse brain lysates by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.
Related Product 1: Amyloid Fibrils (OC) pan-specific antibody (Cat. No.: AB-NN194-1)
Scientific Background: 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. Many degenerative diseases are known to be related to the accumulation of misfolded proteins as amyloid fibres (1, 2). These include the amyloid-β peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimer’s symptomology, the deposition of α-synuclein in the Lewy bodies of Parkinson’s disease, and accumulation of polyglutamine-containing aggregates in Huntington’s disease (2, 3). Amyloid Precursor Protein (APP) is a type-I transmembrane glycoprotein, primarily expressed in the brain, that plays a critical role in synaptic formation, repair, and neuronal signaling. It is the precursor to the amyloid-beta (Ab) peptide, which, when misprocessed, forms pathogenic amyloid plaques in Alzheimer's disease. Abnormal cleavage of APP by beta-secretase and gamma-secretase releases toxic peptides, which aggregate into neurotoxic extracellular plaques. APP features a large extracellular N-terminal domain, a single transmembrane domain, and a short intracellular C-terminal domain (AICD). It is normally highly expressed in the nervous system, and is involved in cell adhesion, copper transport, synaptic plasticity and long-term potentiation. This description may include information annotated by UniProt and/or Google AI.