β Amyloid 1-42 Rabbit mAb

Catalog No.: F3375

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
IHC1:1000

Application
IHC

Source
Rabbit

Reactivity
Mouse, Rat, Human

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

Datasheet & SDS

Biological Description

Specificity
β Amyloid 1-42 Rabbit mAb detects endogenous levels of total β Amyloid 1-42 protein.

Clone
H15J22

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
Amyloid β 1-42 (Aβ42) is a 42–amino acid peptide generated from the amyloid precursor protein (APP) through sequential cleavage by β-secretase and γ-secretase in neurons. Structurally, Aβ42 is highly hydrophobic at its C-terminus, promoting a conformational shift from α-helix to β-sheet that facilitates aggregation into soluble oligomers, protofibrils, and insoluble amyloid fibrils. Aβ42 is expressed primarily in the brain, especially in the neocortex, and is more aggregation-prone and neurotoxic than the shorter Aβ40 form. Functionally, pathological accumulation of Aβ42—particularly as soluble oligomers—is strongly implicated in Alzheimer’s disease pathogenesis by disrupting synaptic signaling, impairing memory, and contributing to plaque formation.

Background

Amyloid β 1-42 (Aβ42) is a 42–amino acid peptide generated from the amyloid precursor protein (APP) through sequential cleavage by β-secretase and γ-secretase in neurons. Structurally, Aβ42 is highly hydrophobic at its C-terminus, promoting a conformational shift from α-helix to β-sheet that facilitates aggregation into soluble oligomers, protofibrils, and insoluble amyloid fibrils. Aβ42 is expressed primarily in the brain, especially in the neocortex, and is more aggregation-prone and neurotoxic than the shorter Aβ40 form. Functionally, pathological accumulation of Aβ42—particularly as soluble oligomers—is strongly implicated in Alzheimer’s disease pathogenesis by disrupting synaptic signaling, impairing memory, and contributing to plaque formation.

References
[1] Chen GF, et al. Acta Pharmacol Sin. 2017 Sep;38(9):1205-1235. [2] Gu L, et al. J Neurochem. 2013 Aug;126(3):305-11.

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

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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%