MABN878

Anti-phospho-Amyloid beta (Ser8) Antibody, clone 1E4E11

clone 1E4E11, from mouse

• 別名: Aβ peptide, Ser8 phosphorylated, Abeta peptide, Ser8 phosphorylated, Amyloid β peptide, Ser8 phosphorylated, Aβ1-40, Ser8 phosphorylated, Aβ1-42, Ser8 phosphorylated, Abeta1-40, Ser8 phosphorylated, Abeta1-42, Ser8 phosphorylated
• UNSPSCコード: 12352203
• eCl@ss: 32160702
• NACRES: NA.41

特性

• 由来生物: mouse
• 品質水準: 100
• 抗体製品の状態: purified immunoglobulin
• 抗体製品タイプ: primary antibodies
• クローン: 1E4E11, monoclonal
• 化学種の反応性: human
• テクニック: ELISA: suitable; immunofluorescence: suitable; immunohistochemistry: suitable; western blot: suitable
• アイソタイプ: IgG1κ
• NCBIアクセッション番号: NP_000475
• UniProtアクセッション番号: P05067
• ターゲットの翻訳後修飾: phosphorylation (pSer8)
• 遺伝子情報: human ... APP(351)

詳細

詳細

Amyloid beta A4 protein (UniProt P05067; also known as ABPP, Alzheimer disease amyloid protein, Amyloid precursor protein, APP, APPI, Cerebral vascular amyloid peptide, CVAP, PN-II, PreA4, Protease nexin-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID 351) in human. Amyloid precursor protein (APP) is initially produced with a signal peptide sequence (a.a. 1-17), the removal of which yields the mature protein with a large extracellular portion (a.a. 18-699), followed by a transmembrane segment (a.a. 700-723) and a cytoplasmic (a.a. 724-770) tail. APP can be further processed by the α-, β-, and γ-secretases in two alternative processing pathways. In the non-amyloidogenic pathway, APP is first cleaved by the plasma membrane-localized α-secretase to generate an N-terminal extracellular sAPPα fragment (a.a. 18-687) and a membrane-bound C-terminal fragment C83 (CTFα), which can be further cleaved by γ-secretase to produce a non-toxic small peptide p3 and a cytoplasmic APP intracellular domain (AICD). In the amyloidogenic pathway, APP undergoes β-cleavage in BACE-1 (β-site APP-cleaving enzyme)-enriched endosomes to generate an N-terminal extracellular sAPPβ fragment (a.a. 18-671) and a membrane-bound C-terminal fragment C99 (CTFβ). Subsequent cleavage of C99 by γ-secretase releases the amyloid β peptides, Aβ1-42 (672-713) & Aβ1-40 (672-711), and AICD. Aβ accumulation in the cortical and hippocampal regions of the brain is a major pathological feature of Alzheimer′s disease (AD). Aβ Ser8 phosphorylation is shown to promote Aβ aggregation into oligomeric and fibrillar assemblies and to prevent Aβ proteolytic clearance by certain proteases.

特異性

Clone 1E4E11 detected Aβ1-40 and Aβ1-42 peptides with phosphorylated Ser8, but not the non-phosphorylated Aβ peptides (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709).

免疫原

Epitope: Abeta pSer8

KLH-conjugated linear peptide corresponding to an amyloid beta peptide-derived sequence with phosphorylated Ser8.

アプリケーション

Research Category
ニューロサイエンス

Research Sub Category
神経変性疾患

Anti-phospho-Amyloid beta (Ser8) Antibody, clone 1E4E11 is an antibody against phospho-Amyloid beta (Ser8) for use in Western Blotting, Enzyme Immunoassay (ELISA), Immunohistochemistry, Immunofluorescence.

Western Blotting Analysis: 2 µg/mL from a representative lot detected 2.5-100 ng of Ser8-phosphorylated synthetic Aβ1-40 peptide, but not non-phosphorylated Aβ1-40 peptide (Courtesy of Dr. Kumar and Prof. Dr. Walter, Department of Neurology, University Bonn, Germany).
Western Blotting Analysis: 2 µg/mL from a representative lot detected phosphorylated oligomeric amyloid beta (pAβ) peptides in 50 µg of brain extract from an 8-month old APP/PS1KI transgenic mouse, but not in extract from an age-matched non-transgenic mouse (Courtesy of Dr. Kumar and Prof. Dr. Walter, Department of Neurology, University Bonn, Germany).
ELISA Analysis: Clone 1E4E11 hybridoma culture supernatant detected the immunogen peptide with phosphorylated Ser8, but not the corresponding non-phosphorylated peptide (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709).
Immunohistochemistry Analysis: A representative lot detected age-dependent phospho-amyloid beta (pAβ) immunoreactivity and localization in paraffin-embedded APP/PS1KI mouse brain sections following antigen retrieval by heat and 88% formic acid treatments (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709).
Immunofluorescence Analysis: A representative lot detected phospho-amyloid beta (pAβ) immunoreactivity in cortical neurons colocalized with that detected with a non-phospho-specific Aβ antibody by dual fluorescent immunohistochemistry staining of paraffin-embedded 2-month old APP/PS1KI mice cotex sections following anigen retrieval by heat and 88% formic acid treatments (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709).
Western Blotting Analysis: A representative lot detected monomeric, dimeric, trimeric, and oligomeric forms of synthetic Aβ1-40 and Aβ1-42 peptides with phosphorylated Ser8, but not the non-phosphorylated Aβ1-40 and Aβ1-42 peptides (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709).
Western Blotting Analysis: A representative lot detected monomeric, dimeric, and oligomeric forms of phosphorylated amyloid beta (pAβ) peptides in brain extracts from 6- and 12-month old APP/PS1KI transgenic mice, but not in brain extracts from age-matched non-transgenic mice (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709).
Note: Formic acid (88%) treatment following heat retrieval is recommended for immunohistochemical detection of aggregated intraneuronal Abeta peptides in brain sections (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709; Christensen, D.Z., et al. (2009). Brain Res. 1301:116-125).

品質

Identity Confirmation by Isotyping Test.

Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG1κ.

ターゲットの説明

~4/8 kDa (monomer/dimer) and greater than 188 kDa (oligomer) observed. 4.514/9.028 kDa (Abeta1-42 monomer/dimer), 4.330/8.660 kDa (Abeta1-40 monomer/dimer) calculated.

物理的形状

Protein G purified.

Format: Purified

Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

保管および安定性

Stable for 1 year at 2-8°C from date of receipt.

その他情報

Concentration: Please refer to lot specific datasheet.

免責事項

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

安全性情報

• 保管分類コード: 12 - Non Combustible Liquids
• WGK: WGK 1
• 引火点(°F): Not applicable
• 引火点(℃): Not applicable