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Human Polyclonal PSENEN Primary Antibody für IP, WB - ABIN152567
Luo, Wang, Li, Kim, Shah, Lee, Thinakaran, Kim, Yu, Xu: PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1. in The Journal of biological chemistry 2003
Human Polyclonal PSENEN Primary Antibody für IF, WB - ABIN2476098
Otto, Koch, Freitag, Freitag, Parnitzke, Abraham, Bartels: [Results of nuclear medical, electroencephalographic, and angiographic examinations after brain tumor operations]. in Psychiatrie, Neurologie, und medizinische Psychologie 1976
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Human Polyclonal PSENEN Primary Antibody für IHC (p), WB - ABIN2476099
Francis, McGrath, Zhang, Ruddy, Sym, Apfeld, Nicoll, Maxwell, Hai, Ellis, Parks, Xu, Li, Gurney, Myers, Himes, Hiebsch, Ruble, Nye, Curtis: aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation. in Developmental cell 2002
Show all 2 Pubmed References
APP (zeige APP Antikörper) substrate occupancy of these three pockets of gamma-secretase occurs after initial substrate binding but precedes catalysis, suggesting a conformational change in substrate may be required for cleavage.
PSENEN mutations can indeed cause a comanifestation of Dowling-Degos disease and acne inversa (AI) that is likely triggered by predisposing factors for AI.
zinc, copper inhibited Abeta (zeige APP Antikörper) production by directly targeting the subunits presenilin and nicastrin (zeige NCSTN Antikörper) in the gamma-secretase complex
PSENEN may play a crucial role in the progression of atopic dermatitis by participating in the Notch (zeige NOTCH1 Antikörper) signaling pathway.
Remarkably, PEN-2 was identified besides nicastrin (zeige NCSTN Antikörper) as additional substrate-binding subunit.
TRPC6 (zeige TRPC6 Antikörper) specifically interacts with APP (zeige APP Antikörper) leading to inhibition of its cleavage by gamma-secretase and reduction in Abeta (zeige APP Antikörper) production.
secondary mutations in presenilin 1 (zeige PSEN1 Antikörper) alone activated the gamma-secretase activity.
Data indicate that familial Alzheimer's disease (FAD (zeige BRCA2 Antikörper)) and control brain samples had similar overall gamma-secretase activity levels, and therefore, loss of overall (endopeptidase) gamma-secretase function cannot be an essential part of the pathogenic mechanism.
We for the first time identify PEN-2 as the causative gene of familial comedones.
The first hydrophobic domain of Pen-2 forms a structure similar to a reentrant loop while the second hydrophobic domain spans the lipid bilayer.
The PSENEN gene is down-regulated in bovine intramuscular fibroblast cells during differentiation into adipocytes.
Cleavage of the Interleukin-11 receptor (zeige IL11RA Antikörper) induces processing of its C-terminal fragments by the gamma-secretase and the proteasome.
the G206D mutation reduced presenilin-1 (zeige PSEN1 Antikörper)-presenilin enhancer 2 interaction, but did not abolish gamma-secretase formation and presenilin-1 (zeige PSEN1 Antikörper) endoproteolysis
Data show that the expression level of presenilin enhancer-2 (Pen-2) is relatively high in central nervous system at the early stages of postnatal development, but declines, gradually in adult mice.
rather than solely being a catalyst for gamma-secretase endoproteolysis, Pen-2 may also stabilize the complex prior to PS1 (zeige PSEN1 Antikörper) endoproteolysis, allowing time for full assembly and proper trafficking.
Pen-2, as well as nicastrin (zeige NCSTN Antikörper) and Aph-1alpha (zeige APH1A Antikörper), is dispensable for presenilin endoproteolysis
Nct (zeige NCSTN Antikörper) has a critical role in the stability and proper intracellular trafficking of other components of the PS1 (zeige PSEN1 Antikörper)/ gamma-secretase complex but not in maintaining the association of PEN-2, APH-1 (zeige APH1A Antikörper), and full-length PS1 (zeige PSEN1 Antikörper)
APH-1 (zeige APH1A Antikörper) stabilizes the presenilin holoprotein in the complex, whereas PEN-2 is required for endoproteolytic processing of presenilin and conferring gamma-secretase activity to the complex.
presenilin, nicastrin (zeige NCSTN Antikörper), APH-1 (zeige APH1A Antikörper), and PEN-2, are present and enriched on phagosome membranes from both murine macrophages and Drosophila S2 phagocytes
Presenilins, which are components of the gamma-secretase protein complex, are required for intramembranous processing of some type I transmembrane proteins, such as the Notch proteins and the beta-amyloid precursor protein. Signaling by Notch receptors mediates a wide range of developmental cell fates. Processing of the beta-amyloid precursor protein generates neurotoxic amyloid beta peptides, the major component of senile plaques associated with Alzheimer's disease. This gene encodes a protein that is required for Notch pathway signaling, and for the activity and accumulation of gamma-secretase.
gamma-secretase subunit PEN-2
, hematopoietic stem/progenitor cells protein MDS033
, presenilin enhancer protein 2
, presenilin enhancer 2
, LRRGT00140 mRNA
, liver regeneration-related protein LRRGT00140
, Presenilin enhancer protein 2 homolog
, presenilin enhancer 2 homolog
, presenilin enhancer protein 2 homolog