β-Amyloid (1-42) (E6D5M) Rabbit mAb (BSA and Azide Free) #82095

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)
Source/Isotype	Rabbit IgG

Application Key:

IHC-Immunohistochemistry
IF-Immunofluorescence

Species Cross-Reactivity Key:

H-Human

Product Information

Product Usage Information

This product is the carrier free version of product #24090. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

Formulation

Supplied in 1X PBS (10 mM Na₂HPO₄, 3 mM KCl, 2 mM KH₂PO₄, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

For standard formulation of this product see product #24090.

Storage

Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

Specificity / Sensitivity

β-Amyloid (1-42) (E6D5M) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total Aβ-42 protein. This antibody does not cross-react with other β-amyloid peptides.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human β-amyloid (1-42) 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).

Database Links

UniProt ID: P05067

Entrez-Gene Id: 351

限制使用

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

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