- Poly8250 (See other available formats)
- Regulatory Status
- Other Names
- Amyloid beta A4 protein, preA4, protease nexin-II, peptidase nexin-II, beta-amyloid peptide, alzheimer disease amyloid protein, cerebral vascular amyloid peptide, APP, Amyloid Precursor Protein
Signet Catalog# 9150-005
Covance Catalog# SIG-39150
- Rabbit Polyclonal IgG
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- Product Citations
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APP (Amyloid Precursor Protein) is a single-pass type I membrane protein expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.
APP functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including the beta-amyloid X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686.
Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides.
- Verified Reactivity
- Antibody Type
- Host Species
- Reactive to the C-terminal fragment of Amyloid Precursor Protein (APP).
- Phosphate-buffered solution; no preservatives or carrier proteins.
- The antibody was purified by affinity chromatography.
- 1.0 mg/ml
- Storage & Handling
- The antibody solution should be stored undiluted between 2°C and 8°C. Please note the storage condition for this antibody has been changed from -20°C to -70°C to between 2°C and 8°C. You can also check your vial or your CoA to find the most accurate storage condition for this antibody. Do not store antibody diluted below 50 µg/mL.
ELISA - Quality tested
WB - Reported in the literature, not verified in house
- Recommended Usage
Each lot of this antibody is quality control tested by ELISA assay.
The optimal working dilution should be determined for each specific assay condition.
• ELISA: 2.5-250ng/mL
- Application Notes
This antibody is effective in ELISA and Western blotting. Other applications are under evaluation.
This product may contain other non-IgG subtypes.
(PubMed link indicates BioLegend citation)
- Pinnix I, et al. 2001. J. Biol. Chem. 276:481. (WB)
- Product Citations
AB_2564886 (BioLegend Cat. No. 825001)
- Biology Area
- Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
- Molecular Family
- Gene ID
- 351 View all products for this Gene ID
- View information about APP C-Terminal Fragment on UniProt.org
|Purified anti-APP C-Terminal Fragment||Poly8250||ELISA,WB|
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Purified anti-APP C-Terminal Fragment