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Tuesday, February 4, 2014

Product Focus: Oligomeric Amyloid beta (oAβ) ELISA from Biosensis

This kit is exclusive to Biosensis and consists of a pre-coated mouse monoclonal anti-Aβ capture antibody (MOAB-2), a biotinylated MOAB-2 detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3’,5,5’-tetramethylbenzidine, TMB) yields a coloured reaction product which is directly proportional to the concentration of o-Aβ present in samples and protein standards. The purpose of this kit is the in vitro qualitative measurement of oligomeric Aβ peptide levels in brain extracts and CSF samples from both transgenic mice and humans relative to a known o-Aβ standard. The inclusion of a highly validated oligomeric standard results in a unique, ready-to-use ELISA kit.

This is the first oligomeric amyloid beta ELISA to take advantage of MOAB-2′s high specificity and avidity for beta amyloid peptides and combine it in a proprietary formulation that allows for the detection of amyloid beta oligomers and complexes present in mouse and human CSF and brain tissue extracts. The ELISA comes complete and ready to use with all the necessary buffers and detection reagents as well as ready-to-polymerize human Aβ 1-42 peptide standards.

Biosensis retains exclusive worldwide rights for MOAB-2 based immunoassays and this is the first of a family of critical Alzheimer’s Disease biomarker assays to be released by Biosensis for neurological disease research. Biosensis’ oAβ ELISA results match that published in the literature for AD patients and transgenic mouse models, and  improves them by providing extremely low backgrounds, superb low end sensitivity, a broad dynamic range and great reproducibility.



Product Code:  BEK-2215-2P
Product Name: Oligomeric Amyloid beta (oAβ) ELISA

Specificity:    Human. MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to Aβ residues 1-4 and is highly specific to amyloid beta peptide.  The Biosensis o-Aβ Elisa detects Aβ oligomers as validated and described by Youmans KL et al (2012).

Other Names:    Beta-APP42; Beta-APP40; Beta-amyloid protein 42; Beta-amyloid protein 40; ABPP; APPI; Amyloid beta A4 protein; MOAB2; MOAB-2; Alzheimer’s antibody; AB40; AB42; abeta.

The ELISA kit box contains 2 x 96 pre-coated strip plates, protein standards, detection reagents, substrate buffer and precise instructions.

Features

  • low background
  • low end sensitivity
  • broad dynamic range
  • reproducibility

Range:    15.6 – 1000 pg/mL
Sensitivity:    30-60 pg/mL (defined as 150% of blank value)
Cross-reactivity:    Rat.


Background

Alzheimer’s disease (AD) is the most common cause of dementia and accounts for 50%-75% of all cases. It has been identified as a protein misfolding disease caused by plaque accumulation of abnormally folded beta amyloid and tau amyloid proteins in the brain.[2] Plaques are made up of small peptides, 39–43 amino acids in length, called beta-amyloid (Aβ) which is a fragment from a larger protein called amyloid precursor protein (APP), which is critical to neuron growth, survival and post-injury repair.[3][4] In AD, a proteolysis process causes APP to be divided into smaller fragments [5] which gives rise to fibrils of beta-amyloid  that deposit outside neurons in dense formations known as senile plaques.[1][6]. Exactly how disturbances of production and aggregation of the beta-amyloid peptide gives rise to the pathology of AD is not known.[7][8]

References

  1. Tiraboschi P, Hansen LA, Thal LJ, Corey-Bloom J. The Importance of Neuritic Plaques and Tangles to the Development and Evolution of AD. Neurology. 2004;62(11):1984–9..
  2. Hashimoto M, Rockenstein E, Crews L, Masliah E. Role of Protein Aggregation in Mitochondrial Dysfunction and Neurodegeneration in Alzheimer’s and Parkinson’s Diseases. Neuromolecular Med.. 2003;4(1–2):21–36.
  3. Priller C, Bauer T, Mitteregger G, Krebs B, Kretzschmar HA, Herms J. Synapse Formation and Function is Modulated by the Amyloid Precursor Protein. J. Neurosci.. 2006;26(27):7212–21.
  4. Turner PR, O’Connor K, Tate WP, Abraham WC. Roles of Amyloid Precursor Protein and its Fragments in Regulating Neural Activity, Plasticity and Memory. Prog. Neurobiol.. 2003;70(1):1–32.
  5. Hooper NM. Roles of Proteolysis and Lipid Rafts in the Processing of the Amyloid Precursor Protein and Prion Protein. Biochem. Soc. Trans.. 2005;33(Pt 2):335–8.
  6. Ohnishi S, Takano K. Amyloid Fibrils from the Viewpoint of Protein Folding. Cell. Mol. Life Sci.. 2004;61(5):511–24.
  7. Van Broeck B, Van Broeckhoven C, Kumar-Singh S. Current Insights into Molecular Mechanisms of Alzheimer Disease and Their Implications for Therapeutic Approaches.Neurodegener Dis. 2007;4(5):349–65..
  8. Huang Y, Mucke L. Alzheimer Mechanisms and Therapeutic strategies. Cell. 2012;148(6):1204-22.

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