Western blot analysis of the indicated amounts of human Aβ-37 peptide using β-Amyloid (1-37 Specific) (D2A6H) Rabbit mAb.
Western blot analysis of brain extracts from 13-month old wild-type and TG2576 mice using β-Amyloid (1-37 Specific) (D2A6H) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower).
Western blot analysis of human Aβ-37, Aβ-38, Aβ-39, Aβ-40, Aβ-42, and Aβ-43 peptides (10 ng) using β-Amyloid (1-37 Specific) (D2A6H) Rabbit mAb (upper) or β-Amyloid (D54D2) XP® Rabbit mAb #8243 (lower).
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
From sample preparation to detection, the reagents you need for your Western Blot are now in one convenient kit: #12957 Western Blotting Application Solutions Kit
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 10
β-Amyloid (1-37 Specific) (D2A6H) Rabbit mAb recognizes the Aβ-37 isoform of the β-amyloid peptides. This antibody does not cross-react with other β-amyloid peptides.
Mouse, Rat, Monkey, Bovine
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxy terminus of human β-amyloid (1-37) peptide.
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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