Confocal immunofluorescent analysis of mouse Tg2576 brain which overexpresses mutant human APP695. Sections were labeled with ASC/TMS1 (D2W8U) Rabbit mAb (Mouse Specific) (Alexa Fluor® 488 conjugate) #17507 (green), β-Amyloid (D54D2) XP® Rabbit mAb (Alexa Fluor® 594 Conjugate) (yellow), and GFAP (GA5) Mouse mAb (Alexa Fluor® 647 Conjugate) #3657 (red). Samples were mounted in ProLong® Gold Antifade Reagent with DAPI #8961 (blue).
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Amyloid (D54D2) XP® Rabbit mAb #8243.
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 (D54D2) XP® Rabbit mAb (Alexa Fluor® 594 Conjugate) recognizes endogenous levels of total β-amyloid peptide (Aβ). The antibody detects several isoforms of Aβ, such as Aβ-37, Aβ-38, Aβ-39, Aβ-40, and Aβ-42. This product detects transgenically expressed human APP in mouse models.Species Reactivity:
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human β-amyloid peptide (Aβ).
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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