Biolegend, 618252, Purified anti-β-Amyloid, 1-16 Recombinant Antibody, 100μg

Alzheimer's disease is characterized by the accumulation of aggregated β-amyloid (Aβ) peptides in senile plaques and vascular deposits. Aβ peptides are derived from amyloid precursor proteins (APP) through sequential proteolytic cleavage of APP by β-secretases and γ-secretases generating diverse Aβ species. Aβ can aggregate to form soluble oligomeric species and insoluble fibrillar or amorphous assemblies. Some forms of the aggregated peptides are toxic to neurons.
100μg
Verified Reactivity: Human
Antibody Type: Recombinant
Host Species: Mouse
Immunogen: β-Amyloid signal peptide residues 1-16
Formulation: Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
Preparation: The antibody was purified by affinity chromatography.
Concentration: 0.5 mg/mL
Storage & Handling: The antibody solution should be stored undiluted between 2°C and 8°C.
Application: IHC-P - Quality tested Direct ELISA, WB - Verified
Recommended Usage: Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 5.0 - 10 µg/mL is suggested. Direct ELISA detects a β-amyloid fragment containing amino acids 1-16. For western blotting, the suggested use of this reagent is 0.25 - 1.0 µg/mL. It is recommended that the reagent be titrated for optimal performance for each application.
RRID: AB_3068053 (BioLegend Cat. No. 618251) AB_3068053 (BioLegend Cat. No. 618252)
Structure: Amyloid precursor protein is a 770 amino acid protein with a molecular mass of ~100 kD. According to the UniProtKB database, APP (ID# P05067) has 11 isoforms (34 to ~90 kD) and the 770 form has been designated as the canonical form. Isoform APP695 is the predominant form expressed in neuronal tissue. Isoforms APP751 and APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Aβ denotes peptides of 36-43 amino acids generated from cleavage of APP by secretases. Aβ has an apparent molecular mass of about 4 kD.
Distribution: Tissue distribution: Primarily nervous system, but also adipose tissue, intestine, and muscle Cellular distribution: Cytosol, endosomes, nucleus, plasma membrane, extracellular, and Golgi apparatus
Function: The normal function of Aβ is not well understood. Several potential physiological roles have been proposed, including: activation of kinase enzymes, protection against oxidative stress, regulation of cholesterol transport, transcription factor, and as an anti-microbial agent.
Biology Area: Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Antigen References: Kumar A, et al. 2015. Pharmacol Rep. 67:195-203. Sadigh-Eteghad S, et al. 2015. Med Princ Pract. 24:1-10. Hampel H, et al. 2015. Expert Rev Neurother. 15:83-105. Puig KL & Combs CK. 2012. Exp Gerontol. 48: 608-11. Selkoe DJ & Hardy J. 2016. EMBO Mol Med. 8:595-608. Walsh DM & Selkoe DJ. 2007. J Neurochem. 101:1172-84.
Gene ID: 351
UniProt: View information about beta-Amyloid 1-16 on UniProt.org
Clone: 6E10.Rec
Regulatory Status: RUO
Other Names: AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2, Amyloid beta A4 protein, preA4, protease, peptidase nexin-II, beta-amyloid peptide, alzheimer disease amyloid protein, cerebral vascular amyloid peptide, APP, Amyloid Precursor Protein
Isotype: Mouse IgG1, κ