Confocal immunofluorescent analysis of brain from the 5XFAD mouse model of Alzheimer's disease using β-Amyloid (1-43 Preferred) (E8C2D) Rabbit mAb (Alexa Fluor® 555 Conjugate) (red pseudocolor), GFAP (GA5) Mouse mAb #3670 (green), and β-Amyloid (D54D2) XP® Rabbit mAb (Alexa Fluor® 647 Conjugate) #42284 (yellow pseudocolor). Samples were mounted in ProLong® Gold Antifade Reagent with DAPI #8961 (blue).
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Amyloid (1-43 Preferred) (E8C2D) Rabbit mAb #32098.
Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibody. Protect from light. Do not freeze.
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Cover sections with 4% formaldehyde dilute in 1X PBS.
NOTE: Formaldehyde is toxic, use only in fume hood.
NOTE: All subsequent incubations should be carried out at room temperature unless otherwise noted in a humid light-tight box or covered dish/plate to prevent drying and fluorochrome fading.
posted November 2006
revised November 2013
Protocol Id: 222
β-Amyloid (1-43 Preferred) (E8C2D) Rabbit mAb (Alexa Fluor® 555 Conjugate) recognizes endogenous levels of total human Aβ-43 protein. This product detects transgenically expressed human APP in mouse models. This antibody weakly cross-reacts with human Aβ-42 protein.
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy of human β-Amyloid (1-43) protein.
Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).
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