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anti-Human APH1A Antibodies:
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Human Polyclonal APH1A Primary Antibody for WB - ABIN549020
Fortini: Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling. in Nature reviews. Molecular cell biology 2002
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Human Polyclonal APH1A Primary Antibody for IHC, ELISA - ABIN1001791
Periz, Fortini: Functional reconstitution of gamma-secretase through coordinated expression of presenilin, nicastrin, Aph-1, and Pen-2. in Journal of neuroscience research 2004
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Human Polyclonal APH1A Primary Antibody for ELISA, WB - ABIN1001792
Selkoe: The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease. in Trends in cell biology 1999
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Human Polyclonal APH1A Primary Antibody for ELISA, WB - ABIN545811
Marlow, Canet, Haugabook, Hardy, Lahiri, Sambamurti: APH1, PEN2, and Nicastrin increase Abeta levels and gamma-secretase activity. in Biochemical and biophysical research communications 2003
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Human Polyclonal APH1A Primary Antibody for IHC (p), WB - ABIN541573
Goutte, Tsunozaki, Hale, Priess: APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. in Proceedings of the National Academy of Sciences of the United States of America 2002
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Human Polyclonal APH1A Primary Antibody for WB - ABIN541572
Ma, Li, Price, Wong: APH-1a is the principal mammalian APH-1 isoform present in gamma-secretase complexes during embryonic development. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2005
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Human Polyclonal APH1A Primary Antibody for ChIP, ICC - ABIN261469
Gu, Chen, Sanjo, Kawarai, Hasegawa, Duthie, Li, Ruan, Luthra, Mount, Tandon, Fraser, St George-Hyslop: APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin.nicastrin complexes. in The Journal of biological chemistry 2003
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Human Polyclonal APH1A Primary Antibody for ELISA, WB - ABIN547945
Spasic, Raemaekers, Dillen, Declerck, Baert, Serneels, Füllekrug, Annaert: Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway. in The Journal of cell biology 2007
Using purified PSEN1/Aph1A gamma-secretase and the APPC99-3XFLAG substrate, authors show that substrate shortening progressively destabilizes the consecutive enzyme-substrate complexes that characterize the sequential gamma-secretase processing of APP; present a unifying model for how PSEN or APP mutations enhance amyloidogenic Abeta production, suggests that environmental factors may increase Alzheimer's Disease risk.
Data show that presenilin 1 (PS1)/anterior-pharynx-defective protein 1 (Aph1b), presenilin 2 (PS2)/Aph1aL, PS2/Aph1aS and PS2/anterior pharynx defective 1 homolog B (Aph1b) gamma-secretase produced amyloid beta peptide (Abeta) with a higher Abeta42+Abeta43-to-Abeta40 (Abeta42(43)/Abeta40) ratio than the other gamma-secretases.
Data show that presenilin 1 (PS1)-containing gamma-secretase complexes were targeted to the plasma membrane, whereas presenilin 2 (PS2)-containing ones were addressed to the trans-Golgi network, to recycling endosomes.
No statistically significant difference was detected either in APOE or APH-1a polymorphisms, not suggesting a strong susceptibility to the development of Alzheimer disease.
analysis of how the conformation of presenilin, Pen-2, Aph-1, and nicastrin affect the function and mechanism of gamma-secretase
A loss of PS/gamma-secretase function to cleave Abeta42(43) may initiate Alzheimer's disease.
We demonstrate that extending the transmembrane domain of the amyloid precursor protein-derived C99 substrate in proximity to the cytosolic face strongly influences gamma-secretase cleavage specificity.
The -980C/G polymorphism in APH-1A promoter confers risk of Alzheimer's disease
Coexpression of wild-type or S-palmitoylation-deficient APH1aL and nicastrin leads to marked stabilization of transgenic presenilin 1 in the brains of double-transgenic mice.
Endogenous Aph-1a and its proteolytic fragment have unique properties for cleavage control that may have implications for gamma-secretase regulation and intracellular distribution.
Co-overexpression of presenilin-1 or APH-1 abrogated gamma-secretase inhibition probably through prevention of the incorporation of CRB2 into the gamma-secretase complex
Aph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substrates
These data indicate that mammalian APH-1 (mAPH-1) along with presenilin 1 and nicastrin is probably a functional component of the gamma-secretase complex required for the intramembrane proteolysis of APP and Notch
APH-1 binds to presenilins and nicastrin and may play a role in maturation of presenilin-nicastrin complexes
Expression of APH-1A increases amyloid beta peptide levels and gamma-secretase activity.
APH-1 and the gamma-secretase complex bind to the transmembrane domain region of nicastrin
Six different polymorphisms have been determined but the polymorphisms in APH-1a/b coding regions are not linked to higher risk for Alzheimer disease in an Italian population.
APH-1 can be processed by several endoproteolytic events and generates a stable C-terminal fragment that associates with nicastrin
conserved transmembrane Gly122, Gly126, and Gly130 in the fourth transmembrane region of APH-1a are part of the membrane helix-helix interaction GXXXG motif and are essential for the stable association of APH-1aL with presenilin, nicastrin, and PEN-2
Only the combined overexpression of presenilin 1 and nicastrin together with APH-1a G122D facilitated the formation of a fully active gamma-secretase complex
This work provides novel evidence for the role of miRNAs in memory formation and demonstrates the implication of APH1a protein in miRNA processing in the adult brain.
Prostaglandin I2 accumulation in neuronal cells activates PKA/CREB and JNK/c-Jun signaling pathways by phosphorylation, which results in APH-1alpha/1beta expression.
Thus, Leda-1/Pianp is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease gamma-secretase.
Abeta oligomers in the cerebrospinal fluid (CSF) further promoted the expression of APH-1alpha/-1beta (by >2.5-fold), which enhances the gamma-cleavage of APP and Abeta deposition during AD progression
Upregulation of PS1/gamma-secretase activity may be a risk factor for late onset sporadic Alzheimer's disease.
ficiency of beta-arrestin1 or inhibition of binding of beta-arrestin1 with APH-1 by small peptides reduced Abeta production without affecting Notch processing
Pen-2, as well as nicastrin and Aph-1alpha, is dispensable for presenilin endoproteolysis
presenilin 1 (PS1)-derived fragments, mature nicastrin, APH-1, and PEN-2, associate with cholesterol-rich detergent insoluble membrane (DIM) domains of non-neuronal cells and neurons
Our findings establish that APH-1a is the major mammalian APH-1 homolog present in presenilin-dependent gamma-secretase complexes during embryogenesis.
Nct has a critical role in the stability and proper intracellular trafficking of other components of the PS1/ gamma-secretase complex but not in maintaining the association of PEN-2, APH-1, and full-length PS1
This gene encodes a component of the gamma secretase complex that cleaves integral membrane proteins such as Notch receptors and beta-amyloid precursor protein. The gamma secretase complex contains this gene product, or the paralogous anterior pharynx defective 1 homolog B (APH1B), along with the presenilin, nicastrin, and presenilin enhancer-2 proteins. The precise function of this seven-transmembrane-domain protein is unknown though it is suspected of facilitating the association of nicastrin and presenilin in the gamma secretase complex as well as interacting with substrates of the gamma secretase complex prior to their proteolytic processing. Polymorphisms in a promoter region of this gene have been associated with an increased risk for developing sporadic Alzheimer's disease. Alternative splicing results in multiple protein-coding and non-protein-coding transcript variants.
anterior pharynx defective 1 homolog A
, gamma-secretase subunit APH-1A
, presenilin-stabilization factor
, anterior pharynx defective 1a homolog
, N-acylaminoacyl-peptide hydrolase