Human APP/Protease Nexin II Pan Specific Antibody Summary
Leu18-Arg336
Accession # NP_958817
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.
Scientific Data
APP/Protease Nexin II in Human Brain. APP/Protease Nexin II was detected in immersion fixed paraffin-embedded sections of human brain (Alzheimer's disease cortex) using Goat Anti-Human APP/Protease Nexin II Pan Specific Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1168) at 1 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to neuronal cell bodies. Staining was performed using our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
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: APP
Amyloid precursor protein (APP) is a type I membrane protein with several human isoforms due to alternative splicing. APP-770, -751, and -733 contain a Kunitz protease inhibitor (KPI) domain (residue 291 - 342) and APP-695 does not. APP is a cell surface molecule with many functions. It can be processed proteolytically in two different pathways. In one pathway, beta - and gamma -secretase cleave at the beta site between residue 670 and 671 and the gamma site between residue 711 and 714 to produce beta ‑amyloid peptide (A beta 40 and A beta 42), a major component in plaques found in brains of patients with Alzheimer's disease (1). The other pathway involves alpha -secretase that cleaves residues between 687 and 688. It is antiamyloidogenic due to its benign character and the prevention of the A beta peptide formation (2). Soluble APP containing the KPI domain, also referred to as protease nexin II, is a potent inhibitor of serine proteases and may have additional functions. For example, it may regulate the contact face of blood coagulation and limit thrombosis specially in brain due to its localization and coagulation factor XI inhibiting activity (3, 4).
- Haass, C. (2004) EMBO J. 23:483.
- Lichtenthaler, S. F. and C. Haass (2004) J. Clin. Invest. 113:1384.
- Badellino, K.O. and P.N. Walsh (2000) Biochemistry 39:4769.
- Xu, F. et al. (2005) Proc. Natl. Acad. Sci USA. 102:18135.
Product Datasheets
Citations for Human APP/Protease Nexin II Pan Specific 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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Absence of microglia promotes diverse pathologies and early lethality in Alzheimer's disease mice
Authors: S Kiani Shab, S Morabito, EP Danhash, A McQuade, JR Sanchez, E Miyoshi, JP Chadarevia, C Claes, MA Coburn, J Hasselmann, J Hidalgo, KN Tran, AC Martini, W Chang Roth, J Pascual, E Head, DA Hume, C Pridans, H Davtyan, V Swarup, M Blurton-Jo
Cell Reports, 2022-06-14;39(11):110961.
Species: Mouse
Sample Types: Tissue Homogenates
Applications: Western Blot -
A small molecule ApoE4-targeted therapeutic candidate that normalizes sirtuin 1 levels and improves cognition in an Alzheimer's disease mouse model
Authors: J Campagna, P Spilman, B Jagodzinsk, D Bai, A Hatami, C Zhu, T Bilousova, M Jun, CJ Elias, J Pham, G Cole, MJ LaDu, ME Jung, DE Bredesen, V John
Sci Rep, 2018-12-04;8(1):17574.
Species: Mouse
Sample Types: Plasma
Applications: ELISA Development -
Sortilin and SorLA Display Distinct Roles in Processing and Trafficking of Amyloid Precursor Protein
Authors: Camilla Gustafsen, Simon Glerup, Lone Tjener Pallesen, Ditte Olsen, Olav M. Andersen, Anders Nykjær et al.
The Journal of Neuroscience
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