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Abeta 40 encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Zusätzlich bieten wir Ihnen Amyloid beta 40 Kits (56) und und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 23 products:
Human Polyclonal Abeta 40 Primary Antibody für ELISA, ICC - ABIN4277269
Esler, Stimson, Fishman, Ghilardi, Vinters, Mantyh, Maggio: Stereochemical specificity of Alzheimer's disease beta-peptide assembly. in Biopolymers 1999
Show all 3 Pubmed References
Human Polyclonal Abeta 40 Primary Antibody für ICC, IF - ABIN152565
Pradines, Hernandez-Rapp, Villa-Diaz, Dakowski, Ardila-Osorio, Haik, Schneider, Launay, Kellermann, Torres, Mouillet-Richard: Pathogenic prions deviate PrP(C) signaling in neuronal cells and impair A-beta clearance. in Cell death & disease 2013
Human Polyclonal Abeta 40 Primary Antibody für IHC, ELISA - ABIN1742443
Christensen, Huettenrauch, Mitkovski, Pradier, Wirths: Axonal degeneration in an Alzheimer mouse model is PS1 gene dose dependent and linked to intraneuronal A? accumulation. in Frontiers in aging neuroscience 2014
Taken together, these results suggest that ApoE4 enhances Abeta (zeige APP Antikörper) inhibition of insulin (zeige INS Antikörper)-stimulated AMPA (zeige GRIA3 Antikörper) receptor function, which accelerates memory impairment in ApoE4xAPP mice.
The authors found that as already shown for oligomeric Abeta (zeige APP Antikörper), also oligomeric Tau can bind to amyloid precursor protein (APP (zeige APP Antikörper)). Moreover, efficient intra-neuronal uptake of oligomeric Abeta (zeige APP Antikörper) and oligomeric Tau requires expression of APP (zeige APP Antikörper).
Recombinant mutant KPI(R13I) domain of ABPP (zeige APP Antikörper) was ineffective in the inhibition of pro-thrombotic proteinases and did not inhibit the clotting of plasma in vitro.
Analysis of biochemical fractions of Alzheimer's disease brain extract indicate that the seeding-activity correlated with the presence of ABETA (zeige APP Antikörper) peptide and ABETA (zeige APP Antikörper)-derived aggregates. In vitro-formed fibrils were also active but their activity was low and depending on the fibril structure and conditions of fibril formation.
A comprehensive understanding of the still undefined contribution of Abeta (zeige APP Antikörper) truncations to the disease pathogenesis and their potential as novel therapeutic targets.
The amyloid hypothesis proposes that Alzheimer's Disease is caused by altered beta-amyloid precursor protein expression or APP (zeige APP Antikörper)-mutation-induced Ab aggregation, following an imbalance between Ab production and Ab clearance.
Phosphorylation of amyloid precursor protein by mutant LRRK2 promotes AICD activity and neurotoxicity in Parkinson's disease.
Mass spectrometry analysis of APP (zeige APP Antikörper) intracellular domains revealed differential processing of APP (zeige APP Antikörper)-C83, APP (zeige APP Antikörper)-C89, and APP (zeige APP Antikörper)-C99 by gamma-secretase already at the epsilon-cleavage stage. This mechanistic insight could aid in developing substrate-targeted modulators of APP (zeige APP Antikörper)-C99 processing to specifically lower the Abeta42:Abeta40 ratio without compromising gamma-secretase function.
enzymes known to act in other metabolic pathways, such as meprin beta (zeige MEP1B Antikörper), have been found to cleave APP (zeige APP Antikörper) to yield products known to participate in AD pathologies. This review provides an overview of current knowledge of conventional and novel APP (zeige APP Antikörper) processing.
study provides molecular insights into the design of amyloidogenic inhibitors to cure various neurodegenerative and amyloid-associated diseases, as NABi would regulate aggregation of other toxic beta-sheet proteins other than Abeta (zeige APP Antikörper).
This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.
alzheimer disease amyloid protein
, amyloid beta A4 protein
, beta-amyloid peptide
, cerebral vascular amyloid peptide
, peptidase nexin-II
, protease nexin-II