β Amyloid 1-40 Rabbit mAb

Catalog No.: F2823

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:5000

Application
WB, IHC, I-ELISA

Reactivity
Human

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
86 kDa 4 kDa, 86 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
β Amyloid 1-40 Rabbit mAb detects the Aβ-40 isoform of the β-amyloid peptides.

Clone
G17F9

Synonym(s)
A4, AD1, APP, Amyloid-beta precursor protein, ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta (A4) precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II, CVAP, PN-II

Background
β-Amyloid 1-40 (Aβ40) is a 40-amino-acid peptide generated from the amyloid precursor protein (APP), a type I transmembrane glycoprotein highly expressed in neurons, through sequential cleavage by β-secretase and γ-secretase in the amyloidogenic pathway. Structurally, Aβ40 is intrinsically unstructured in solution but can adopt α-helical or β-sheet conformations depending on the environment; its hydrophobic C-terminal region is crucial for aggregation, while the N-terminal segment is more polar and solvent-exposed. In the healthy brain, APP and its cleavage products, including Aβ40, are involved in synaptic function, neuronal development, and signaling, but excessive Aβ40—especially when misfolded into β-sheet–rich oligomers and fibrils—contributes to amyloid plaque formation, neurotoxicity, and the pathogenesis of Alzheimer’s disease.

Background

β-Amyloid 1-40 (Aβ40) is a 40-amino-acid peptide generated from the amyloid precursor protein (APP), a type I transmembrane glycoprotein highly expressed in neurons, through sequential cleavage by β-secretase and γ-secretase in the amyloidogenic pathway. Structurally, Aβ40 is intrinsically unstructured in solution but can adopt α-helical or β-sheet conformations depending on the environment; its hydrophobic C-terminal region is crucial for aggregation, while the N-terminal segment is more polar and solvent-exposed. In the healthy brain, APP and its cleavage products, including Aβ40, are involved in synaptic function, neuronal development, and signaling, but excessive Aβ40—especially when misfolded into β-sheet–rich oligomers and fibrils—contributes to amyloid plaque formation, neurotoxicity, and the pathogenesis of Alzheimer’s disease.

References
https://pubmed.ncbi.nlm.nih.gov/28713158/ https://pubmed.ncbi.nlm.nih.gov/23406382/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%