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β-Amyloid (1-37) (D2A6H) Rabbit mAb (Biotinylated) #12356

Filter:
  • WB
Western Blotting Image 1: β-Amyloid (1-37) (D2A6H) Rabbit mAb (Biotinylated)
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) (D2A6H) Rabbit mAb (upper) or β-Amyloid (D54D2) XP® Rabbit mAb #8243 (lower).

To Purchase # 12356

Supporting Data

REACTIVITY H
SENSITIVITY Endogenous
MW (kDa) 4
Source/Isotype Rabbit IgG
Application Key:
  • WB-Western Blotting 
Species Cross-Reactivity Key:
  • H-Human 
  • Related Products

Product Information

Product Description

This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Amyloid (1-37) (D2A6H) Rabbit mAb #12467.
MW (kDa) 4

Product Usage Information

Application Dilution
Western Blotting 1:1000

Storage

Supplied in 136 mM NaCl, 2.6 mM KCI, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibodies.

Protocol

Specificity / Sensitivity

β-Amyloid (1-37) (D2A6H) Rabbit mAb (Biotinylated) recognizes the Aβ-37 isoform of the β-amyloid peptides. This antibody does not cross-react with other β-amyloid peptides.

Species Reactivity:

Human

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Mouse, Rat, Monkey, Bovine

Source / Purification

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.

Background

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).

Pathways

Explore pathways related to this product.


For Research Use Only. Not For Use In Diagnostic Procedures.
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