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β-Amyloid Antibody

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  • Cell Signaling Technology已认证
  • USA
  • 2025年08月31日
  • W, IHC-P, IF-P
  • Rabbit
  • H
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 抗体英文名：

      β-Amyloid Antibody

    • 抗原：

      synthetic peptide corresponding to residues at the amino terminus of human beta-amyloid peptides

    • 应用范围：

      W, IHC-P, IF-P

    • 宿主：

      Rabbit

    • 保质期：

      详见说明书

    • 供应商：

      CST

    • 适应物种：

      H

    • 库存：

      大量

    • 级别：

      详见MSDS文件

    • 是否单克隆：

      2

    • 保存条件：

      -20°c

    • 规格：

      40 ul (4 western blots)/100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格：产品价格：￥请询价
    规格：40 ul (4 western blots)产品价格：￥请询价
    规格：100 ul (10 western blots)产品价格：￥请询价
    规格：carrier free & custom formulation / quantity产品价格：￥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)  IF-P=Immunofluorescence (Paraffin)
    Reactivity Key:  H=Human
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W IHC-P IF-P H Endogenous 5 Rabbit
    Protocols
    Specificity / Sensitivity

    beta-Amyloid Antibody detects several isoforms of beta-amyloid peptide (Abeta), such as Abeta-40, Abeta-42 etc, regardless of phosphorylation state.
    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the amino terminus of human beta-amyloid peptides. Antibodies are purified by protein A and peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of human A-beta-40 and A-beta-42 peptides (1-5 ng), using beta-Amyloid Antibody.

    IHC-P (paraffin)

    IHC-P (paraffin)

    Immunohistochemical analysis of paraffin-embedded Alzheimer's brain, using beta-Amyloid Antibody.

    IF-P

    IF-P

    Confocal immunofluorescent analysis of human Alzheimer's brain, using beta-Amyloid Antibody (red) and Tau (Tau46) Mouse mAb #4019 (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
    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 (Aβ), 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 (AD) (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (at 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).

    1. Selkoe, D.J. (1996) J Biol Chem 271, 18295-8.
    2. Caporaso, G.L. et al. (1992) Proc Natl Acad Sci USA 89, 3055-9.
    3. Hung, A.Y. and Selkoe, D.J. (1994) EMBO J 13, 534-42.
    4. Suzuki, T. et al. (1994) EMBO J 13, 1114-22.
    5. Ando, K. et al. (1999) J Neurosci 19, 4421-7.
    6. Iijima, K. et al. (2000) J Neurochem 75, 1085-91.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !
    Companion Products

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

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    • Effects of the β-Amyloid Peptide on Membrane Ion Permeability

      Several lines of evidence suggest a role for membrane ion channels in the neurotoxic effects of the β-amyloid peptide (Aβ). This chapter describes the electrophysiological techniques that can be employed to isolate and record specific membrane

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    • Development of Neoepitope Antibodies Against the β-Secretase Cleavage Site in the Amyloid Precursor Protein

      A detailed understanding of the biochemical events leading to the proteolytic excision of the β-amyloid peptide (A β) from the amyloid precursor protein (APP) has eluded many researchers. This is largely because the measurement of the various APP

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    β-Amyloid Antibody
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