General description
Amyloid beta A4 protein (UniProt: P05067; also known as ABPP, APPI. APP, APP, Alzheimer disease amyloid protein, Amyloid precursor protein, Beta-amyloid precursor protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID: 351) in human. Deposition of Amyloid beta (Ab) is an early event in the pathogenesis of Alzheimer s disease (AD). Ab peptides originate from the proteolytic cleavage of the amyloid precursor protein (APP). APPs are cell surface protein that are internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. The beta-secretase cleaves APP between residues Met671 and Asp672 and yields sAPP beta and C99. Following the beta-secretase cleavage, a second cleavage occurs at the C-terminus of Ab peptide that releases Ab from C99. This cleavage occurs in the vicinity of residue 712 of the C-terminus. The gamma-secretase can cleave the C-terminal region at either Val711 or Ile713 to produce the shorter Ab peptide (Ab1-40) or the longer Ab peptide (Ab1-42). Ab1-42 occurs more frequently and forms fibrillar aggregates far more readily than the Ab1-40 peptide. Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu2+ and Fe3+ to Cu+ and Fe2+, respectively. Abeta42 is a more effective reductant than beta-amyloid 40. From a physiological point of view, it functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. It is also involved in cell mobility and transcription regulation through protein-protein interactions and can promote transcription activation through binding to APBB1-KAT5.
Specificity
This polyclonal antibody detects amyloid precursor protein in human Alzheimer′s disese brain. It targets an epitope within 9 amino acids in the vicintiy of APP585 in the C-terminal region.
Immunogen
A linear peptide corresponding to 9 amino acids from the C-terminal region of human Amyloid beta A4 protein.
Epitope: extracellular domain
Application
Anti-APP585C, Cat. No. ABN1641, is a highly specific rabbit polyclonal antibody that targets Amyloid beta A4 protein and has been tested in Immunohistochemistry (Paraffin) and Western Blotting.
Research Category
Neuroscience
Western Blotting Analysis (WB): A 1:1000 Dilution of this antibody detected Amyloid beta A4 protein in 5XFAD and 5XFAD/AEP-/- mouse brain lysate.
Western Blotting Analysis (WB): A Dilution of this antibody detected Amyloid beta A4 protein in PMID 26549211 .
Immunohistochemistry Analysis (IHC): A Dilution of this antibody detected Amyloid beta A4 protein in PMID 26549211 .
Immunohistochemistry Analysis (IHC): A 1:200 Dilution of this antibody detected Amyloid beta A4 protein in 5XFAD familial AD transgenic mouse brain.
Quality
Evaluated by Immunohistochemistry in human Alzheimer′s diseased human brain tissue.
Immunohistochemistry Analysis: A 1:200 dilution of this antibody detected APP585C in Alzheimer′s diseased human brain tissue.
Target description
10 kDa calculated.
Physical form
Rabbit polyclonal antiserum with 0.05% sodium azide.
Unpurified
Storage and Stability
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Other Notes
Concentration: Please refer to lot specific datasheet.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.