Anti-Amyloid Precursor Protein (Human/Mouse) mAb

  • Applications
    • WB
  • Target Amyloid Precursor
  • Host Species Mouse
  • Species Reactivities Human, Mouse
  • Code # M009-3
  • Size 100 μg
  • Price


Alzheimer's disease (AD) is the most common form of dementia in the elderly. The neuropathological hallmarks are neurofibrillary tangles and senile plaques. The major protein component of the plaques consists of 39-42 amino acids peptide (b-amyloid/Ab). Ab occurs in two predominant forms with different COOH-termini, Ab 40 and Ab 42, and overproduction of Ab 42 has been suggested to be the cause of familial earlyonset AD. Ab generation depends on proteolytic cleavage of the amyloid precursor protein (APP) by two proteases: b-secretase and g-secretase. Recent study suggested that a transmembrane aspartic protease, termed b-site APP-cleaving enzyme (BACE), functionally acts as the b-secretase.
  • Antibody Type:
  • Application:
  • Clone Number:
  • Conjugate:
  • Description:

    Monoclonal Antibody of 100 μg targeting Amyloid Precursor Protein for WB.

  • Formulation:
    This antibody is lyophilized form. Prepare a stock solution by dissolving the lyophilized antibody in 100 mL of distilled water. After reconstitution, the IgG concentration should be 1 mg/mL in PBS (pH 7.2)/1% sucrose, 0.09% NaN3.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Host Species:
  • Immunogen:
    APP695 synthetic peptides (18-38 aa) (LEVPTDGNAGLLAEPQIAMFC)
  • Isotype:
  • Product Type:
  • Reactivity:
    This antibody reacts with Amyloid Precursor Protein on Western blotting
  • Research Area:
  • Short Description:

    Amyloid Precursor Protein Monoclonal Antibody.

  • Size:
    100 μg
  • Species Reactivity:
    Human, Mouse
  • Storage Temperature:
  • Target:
    Amyloid Precursor
  1. Gylys KH et al. Synaptic changes in Alzheimer's disease: increased amyloid-beta and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence. Am J Pathol. 165, 1809-1817 (2004),
  2. Sakai T and Hohjoh H. Gene silencing analyses against amyloid precursor protein (APP) gene family by RNA interference. Cell Biol Int. 30, 952-956 (2006),
  3. Sokolow S et al. AD synapses contain abundant A?A monomer and multiple soluble oligomers, including a 56-kDa assembly. Neurobiol Aging. 33, 1545-1555 (2012)
  1. Gylys, K. H., et al., Am. J. Pathol. 165, 1809-1817 (2004)
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  3. Selkoe, D. J., et al., Cell 58, 611-612 (1989)
  4. Kang, H., et al., Nature 325, 733-736 (1987)