APP Antibody (AB42-5) [Unconjugated]

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Recombinant Human Amyloid beta protein was serially diluted 2-fold and captured by Mouse Anti-Human Amyloid beta (aa1-42) Monoclonal Antibody (Catalog # MAB9618 or Catalog # MAB9618R) coated on a Clear ...read more
Recombinant Human Amyloid beta protein was serially diluted 2-fold and captured by Mouse Anti-Human Amyloid beta (aa1-40) Monoclonal Antibody (Catalog # MAB96181 or Catalog # MAB96181R) coated on a Clear Polystyrene ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications ELISA
Clone
AB42-5
Clonality
Monoclonal
Host
Mouse
Conjugate
Unconjugated

Order Details

View Available Formulations
Catalog# & Formulation Size Price

APP Antibody (AB42-5) [Unconjugated] Summary

Immunogen
Recombinant protein to Fibrillar Amyloid beta 1-42 peptide
Specificity
Detects Human APP/Protease Nexin II (amino acids 1-11 of Amyloid beta ) in direct ELISAs.
Source
N/A
Isotype
IgG
Clonality
Monoclonal
Host
Mouse
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

Applications/Dilutions

Dilutions
  • ELISA
Control
TOR/mTOR Knockout 293T Cell Lysate

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Reconstitution Instructions
Reconstitute at 0.5 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for APP Antibody (AB42-5) [Unconjugated]

  • Abeta
  • amyloid beta (A4) precursor protein-binding, family B, member 2
  • amyloid beta A4 precursor protein-binding family B member 2
  • Amyloid beta precursor protein
  • Amyloid beta
  • APP
  • beta Amyloid
  • beta-amyloid peptide
  • Protease Nexin II

Background

Amyloid Precursor Protein (APP) is a type I transmembrane protein that is ubiquitously expressed on cell surfaces. It undergoes complex proteolytic processing and is cleaved by alpha-, beta-, and gamma-Secretases to generate soluble APP alpha, soluble APP beta, and Amyloid beta (A beta) fragments of several lengths. One of these fragments, A beta 42, generated by beta- and gamma-Secretase activities, has been implicated in Alzheimer's disease. Aberrantly high levels of this peptide form and accumulate in the brains of Alzheimer's disease patients to create the senile plaques characteristic of the disease.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Publications for APP Antibody (MAB96182) (0)

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Product General Protocols

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FAQs for APP Antibody (MAB96182) (0)

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Control Lysate(s)

Secondary Antibodies

 

Isotype Controls

Other Available Formats

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FANCD2 and DNA damage repair
Fanconi anemia (FA) is a genetically inherited disorder that yields cytogenetic instability, hypersensitivity to DNA crosslinking compounds and defective DNA repair. A variety of genes have been identified within the FA pathway that are referred t...  Read full blog post.

Beta Amyloid Neurotoxicity and Alzheimer's Disease
A major histopathological hallmark of Alzheimer's disease (AD) is the presence of amyloid deposits in the parenchyma of the amygdala, hippocampus, and neocortex. The principal component of amyloid is beta amyloid (AB). The pathologic accumulation of A...  Read full blog post.

ApoE: The Key to Preventing Alzheimer's Disease?
Apolipoprotein E also known as ApoE is a 36kDa protein that is expressed in all lipoprotein fractions in plasma. This protein is produced in high quantities in the liver, brain, spleen, lung and kidney. The function of APOE is to mediate the binding,...  Read full blog post.

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