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#10379 Anti-Human Amyloidβ E22P (11A1) Mouse IgG MoAb

  • IHC
Intended Use:
Research reagents
Application:
WB, IP, IHC
Package Size1:
50μg
Package Size2:
5μg
Note on Application Abbreviations
WB:Western Blotting
IP:Immunoprecipitation
IHC:Immunohistochemistry

※ The product indicated as "Research reagents" in the column Intended Use cannot be used
  for diagnostic nor any medical purpose.
※ The datasheet listed on this page is sample only. Please refer to the datasheet
  enclosed in the product purchased before use.

Product Overview

Product Overview

Product Code 10379
Product Name Anti-Human Amyloidβ E22P (11A1) Mouse IgG MoAb
Intended Use Research reagents
Application WB, IP, IHC
Species Human
Immunizing antigen Synthetic peptide of E22P- Amyloidβ10-35 part
Source Mouse-Mouse hybridoma (X63 - Ag 8.653 × BALB/c mouse spleen cells)
Clone Name 11A1
Subclass IgG1
Purification Method Protein A purified
Specificity Reacts with native human Amyloidβ 1-40, 1-42
Package Form Lyophilized product from PBS containing 1 % BSA and 0.05 % NaN3
Storage Condition 2 - 8℃
Poisonous and Deleterious Substances Applicable
Cartagena Not Applicable
Package Size 1 50μg
Package Size 2 5μg
Remarks1 The commercial use of products without our permission is prohibited. Please make sure to contact us and obtain permission.

Product Description

Product Description

Alzheimer’s disease (AD) is characterized by the presence of extracellular plaques and intracellular neurofibrillary tangles (NFTs) in the brain. Aggregation of the 42-mer amyloid β-protein (Aβ42) plays a critical role in the pathogenesis of AD. Shirasawa and Irie et. al have proposed a toxic conformer with a turn at positions 22 and 23, as well as a nontoxic conformer with a turn at positions 25 and 26, in Aβ42 aggregates from systematic proline scanning and solid-state NMR studies. This monoclonal antibody named 11A1 was developed for toxic Aβ42, using E22P-Aβ10-35, a minimum moiety for neurotoxicity containing the turn at positions 22 and 23, for the generation. Immunohistochemical studies showed that not only extracellular but intracellular amyloid was stained in human AD brains, which suggest that 11A1 could detect toxic oligomers of Aβ with the turn at positions 22 and 23.

References

References

Note: Retrieve by PMID number in displayed by abstract: http://www.ncbi.nlm.nih.gov

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