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

Species Reactivity	Key Applications	Host	Format	Antibody Type
H	WB, ELISA, IHC, IF	M	Purified	Monoclonal Antibody

Species Reactivity

Key Applications

Host

Format

Antibody Type

WB, ELISA, IHC, IF

Purified

Monoclonal Antibody

Description
Catalogue Number	MABN878
Description	Anti-phospho-Amyloid beta (Ser8) Antibody, clone 1E4E11
Alternate Names	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
Background Information	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.

Description

Catalogue Number

MABN878

Description

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

Alternate Names

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

Background Information

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.

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

Product Information

Format

Purified

Presentation

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

Applications
Application	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.
Key Applications	Western Blotting Enzyme Immunoassay (ELISA) Immunohistochemistry Immunofluorescence
Application Notes	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).

Applications

Application

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.

Key Applications

Western Blotting
Enzyme Immunoassay (ELISA)
Immunohistochemistry
Immunofluorescence

Application Notes

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).

Biological Information
Immunogen	KLH-conjugated linear peptide corresponding to an amyloid beta peptide-derived sequence with phosphorylated Ser8.
Epitope	Abeta pSer8
Clone	1E4E11
Concentration	Please refer to lot specific datasheet.
Host	Mouse
Specificity	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).
Isotype	IgG1κ
Species Reactivity	Human
Antibody Type	Monoclonal Antibody
Entrez Gene Number	NP_000475
Gene Symbol	APP A4 AD1
Purification Method	Protein G purified.
UniProt Number	P05067
Molecular Weight	~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.

Biological Information

Immunogen

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

Epitope

Abeta pSer8

Clone

1E4E11

Concentration

Please refer to lot specific datasheet.

Host

Mouse

Specificity

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).

Isotype

IgG1κ

Species Reactivity

Human

Antibody Type

Monoclonal Antibody

Entrez Gene Number

NP_000475

Gene Symbol

Purification Method

Protein G purified.

UniProt Number

P05067

Molecular Weight

~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.

Product Usage Statements
Quality Assurance	Identity Confirmation by Isotyping Test. Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG1κ.
Usage Statement	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.

Product Usage Statements

Quality Assurance

Identity Confirmation by Isotyping Test.

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

Usage Statement

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.

Storage and Shipping Information
Storage Conditions	Stable for 1 year at 2-8°C from date of receipt.

Storage and Shipping Information

Storage Conditions

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

Packaging Information
Material Size	100 μg

Packaging Information

Material Size

100 μg

实验耗材

分子生物学试剂

蛋白与免疫学

生化试剂

细胞及检测试剂

色谱及层析

仪器设备

实验服务

办公用品

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

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