A3356
Anti-Beta (β)-Amyloid antibody
rabbit polyclonal
別名:
Anti-A4 AMYLOID PROTEIN, Anti-ABETA, Anti-ABPP, Anti-AD1, Anti-AMYLOID BETA A4, Anti-AMYLOID-BETA PROTEIN (ABP), Anti-APPI
製品名
抗β-アミロイド (22-35) ウサギ宿主抗体, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~4 kDa
species reactivity
rat, human, mouse
packaging
antibody small pack of 25 μL
technique(s)
indirect ELISA: 0.2-0.4 μg/mL using β-amyloid peptide (22-35)
western blot: 0.25-0.5 μg/mL using β-amyloid peptide (1-40)
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... APP(351)
mouse ... App(11820)
rat ... App(54226)
Application
Rabbit anti-β-amyloid (22-35) antibody can be used for ELISA at a concentration of 0.2-0.4μg/mL using β-amyloid peptide (22-35). The product can also be used for western blot at 0.25-0.5μg/mL using β-amyloid peptide (1-40).
Anti-β-Amyloid (22-35) antibody produced in rabbit has been used in:
- western blot
- dot-blot assay
- indirect enzyme linked immunosorbent assay (ELISA)
Biochem/physiol Actions
Secreted Aβ lead to synaptic and neuritic compromise and glial activation. Aggregates of amyloid β peptide are found deposited in the brains of Alzheimer′s patients. Aβ(25-35) and Aβ(22-35) fragments are highly toxic segments of β-amyloid peptides that promote inflammatory processes in astrocytes and fibrillary aggregation of Aβ, thus representing a promising therapeutic target for Alzheimer′s.
Disclaimer
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.
General description
Rabbit anti-β-amyloid (22-35) antibody specifically recognizes β-amyloid (22-35), β-amyloid (25-35), β-amyloid (1-40) and β-amyloid (1-42) and does not react with β-amyloid (32-35) and β-amyloid (35-25) by ELISA. The antibody detects β-amyloid (1-40) by immunoblotting (approx. 4kDa). Staining of the β-amyloid (1-40) band in immunoblotting is specifically inhibited by the immunizing peptide.
Cleavage of the amyloid precursor protein (APP) by γ-secretase produces the small fragment amyloid β (Aβ) peptide. Cleavage of APP occurs mostly at residue 40 but to a lesser extent residue 42. The amyloid β peptide contains a ~100 kDa soluble N-terminal fragment, and intracellular C-terminal fragments (CTFs) bearing the complete Aβ domain.
Proteolytic cleavage of the amyloid precursor protein (APP) produces the small fragment amyloid β peptide. Cleavage of APP occurs mostly at residue 40 but to a lesser extent residue 42. Aggregates of amyloid β peptide are found deposited in the brains of Alzheimer′s patients.
Immunogen
synthetic peptide corresponding to amino acids 22-35 of human β-amyloid (1-40) fragment, conjugated to KLH. This sequence corresponds to amino acids 693-706 of the human amyloid precursor protein APP, and is identical in mouse and rat APP.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide and 1% bovine serum albumin.
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保管分類
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
IL-1beta, TNF-alpha and Sambucus nigra Reactive Serum Proteins as Biomarkers of Mild Cognitive Impairment and Alzheimer Disease Progression
Castillo LM< et al.
Advances in Alzheimer's disease, 4(04), 99-99 (2015)
Mechanisms of Amyloid-beta Peptide Clearance: Potential Therapeutic Targets for Alzheimer's Disease
Yoon SS, et al.
Biomolecules & Therapeutics, 20, 245-245 (2012)
Yuancheng Li et al.
ACS biomaterials science & engineering, 5(7), 3595-3605 (2019-07-08)
Alzheimer's disease (AD) is a growing global healthcare burden affecting the aging population and society. Given the lack of effective treatment to AD, early detection at the prodromal stage and timely monitoring of changes during progression are considered the best
Lukas P Feilen et al.
eLife, 11 (2022-05-18)
Cleavage of membrane proteins in the lipid bilayer by intramembrane proteases is crucial for health and disease. Although different lipid environments can potently modulate their activity, how this is linked to their structural dynamics is unclear. Here, we show that
Mechanisms of transthyretin inhibition of $\beta$-amyloid aggregation in vitro
Li X, et al.
The Journal of Neuroscience, 33(50), 19423-19433 (2013)
関連コンテンツ
Instructions
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