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Abeta encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Zusätzlich bieten wir Ihnen beta Amyloid Antikörper (274) und und viele weitere Produktgruppen zu diesem Protein an.
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Taken together, these results suggest that ApoE4 enhances Abeta (zeige APP ELISA Kits) inhibition of insulin (zeige INS ELISA Kits)-stimulated AMPA (zeige GRIA3 ELISA Kits) receptor function, which accelerates memory impairment in ApoE4xAPP mice.
The authors found that as already shown for oligomeric Abeta (zeige APP ELISA Kits), also oligomeric Tau can bind to amyloid precursor protein (APP (zeige APP ELISA Kits)). Moreover, efficient intra-neuronal uptake of oligomeric Abeta (zeige APP ELISA Kits) and oligomeric Tau requires expression of APP (zeige APP ELISA Kits).
Reco (zeige APP ELISA Kits)mbinant mutant KPI(R13I) domain of ABPP was ineffective (zeige APP ELISA Kits)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 ELISA Kits) peptide and ABETA (zeige APP ELISA Kits)-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 ELISA Kits) 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 ELISA Kits)-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 ELISA Kits) intracellular domains revealed differential processing of APP (zeige APP ELISA Kits)-C83, APP (zeige APP ELISA Kits)-C89, and APP (zeige APP ELISA Kits)-C99 by gamma-secretase already at the epsilon-cleavage stage. This mechanistic insight could aid in developing substrate-targeted modulators of APP (zeige APP ELISA Kits)-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 ELISA Kits), have been found to cleave APP (zeige APP ELISA Kits) to yield products known to participate in AD pathologies. This review provides an overview of current knowledge of conventional and novel APP (zeige APP ELISA Kits) 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 ELISA Kits).
Activation of CaMKIV (zeige CAMK4 ELISA Kits) by soluble amyloid-beta1-42 impedes trafficking of axonal vesicles and impairs activity-dependent synaptogenesis
Abpp (zeige APP ELISA Kits) /KPI(R13I) mutant mice were similarly deficient as Abpp (zeige APP ELISA Kits) knock out mice in regulating cerebral thrombosis in experimental models of carotid artery thrombosis and intracerebral hemorrhage.
The cognitive function of APP (zeige APP ELISA Kits)/PS1 (zeige PSEN1 ELISA Kits) mice was impaired at 10months of age; moreover, the hypermetabolic state identified in various brain regions at 5months of age was also significantly decreased.
APP (zeige APP ELISA Kits) heterozygosity results in greater decreases of cortical APP (zeige APP ELISA Kits) in Transgenic (Tg) versus non-Tg mice. Mutant huntingtin (zeige HTT ELISA Kits) transgenic mice develop brain iron accumulation as a result of greater suppression of APP (zeige APP ELISA Kits) levels. Elevated brain iron in Tg mice was associated with a decline in motor endurance consistent with a disease promoting effect of iron in the YAC128 model of human Huntington's Disease.
Data show that exosomal amyloid precursor protein C-terminal fragments (APP-CTFs) and bis(monoacylglycero)phosphate (BMP) as candidate biomarkers diagnostic of endolysosomal dysfunction associated with neurodegenerative disorders.
Conducted in vivo extracellular recording to investigate cholinergic compound action potentials of the superior cervical ganglion (SCG) in APP (zeige APP ELISA Kits)(-/-) and littermate wild-type (WT) mice; found that APP (zeige APP ELISA Kits) not only regulates presynaptic activity, but also affects postsynaptic function at cholinergic synapses in SCG; also alpha4beta2 and alpha7 nicotinic acetylcholine receptors are reduced in the absence of APP (zeige APP ELISA Kits).
App (zeige APP ELISA Kits)-KI mouse lines with different levels of pathophysiology are useful models of AD.
Loss of Abpp (zeige APP ELISA Kits) is associated with cognitive impairment.
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
, amyloid beta (A4) precursor protein (peptidase nexin-2, Alzheimer disease)
, amyloid beta (A4) precursor protein (protease nexin-II, Alzheimer disease)
, beta-amyloid precursor protein
, alzheimer disease amyloid A4 protein homolog
, amyloid beta (A4) precursor protein (peptidase nexin-II, Alzheimer disease)
, amyloid A4
, amyloidogenic glycoprotein
, protease nexin II