Human/Mouse APLP-1 Antibody Summary
Gln34-Glu580
Accession # P51693
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 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.
Background: APLP-1
APLP-1 is a transmembrane metalloprotein that is expressed in central neurons. Similar to APP and APLP-2, APLP-1 is susceptible to cleavage by various secretases, generating multiple fragments from the extracellular and intracellular domains. These include peptides similar to the amyloidogenic A beta peptides and a cytoplasmic fragment that associates with Fe65 family proteins and functions as a transcriptional activator. The extracellular domain contains heparin and collagen binding regions and is 89% identical between human and mouse.
Product Datasheets
Citations for Human/Mouse APLP-1 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 3
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Biochemical assessment of precuneus and posterior cingulate gyrus in the context of brain aging and Alzheimer's disease.
Authors: Maarouf C, Kokjohn T, Walker D, Whiteside C, Kalback W, Whetzel A, Sue L, Serrano G, Jacobson S, Sabbagh M, Reiman E, Beach T, Roher A
PLoS ONE, 2014-08-28;9(8):e105784.
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Molecular Differences and Similarities between Alzheimer's Disease and the 5XFAD Transgenic Mouse Model of Amyloidosis
Authors: Chera L. Maarouf, Tyler A. Kokjohn, Charisse M. Whiteside, MiMi P. Macias, Walter M. Kalback, Marwan N. Sabbagh et al.
Biochemistry Insights
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Tau and other proteins found in Alzheimer's disease spinal fluid are linked to retromer-mediated endosomal traffic in mice and humans.
Authors: Simoes S, Neufeld J. L, et al.
Sci Transl Med
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