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Human Polyclonal PSENEN Primary Antibody for 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 for 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
Show all 2 Pubmed References
Human Polyclonal PSENEN Primary Antibody for 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 (show APP Antibodies) 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 (show APP Antibodies) production by directly targeting the subunits presenilin and nicastrin (show NCSTN Antibodies) in the gamma-secretase complex
PSENEN may play a crucial role in the progression of atopic dermatitis by participating in the Notch (show NOTCH1 Antibodies) signaling pathway.
Remarkably, PEN-2 was identified besides nicastrin (show NCSTN Antibodies) as additional substrate-binding subunit.
TRPC6 (show TRPC6 Antibodies) specifically interacts with APP (show APP Antibodies) leading to inhibition of its cleavage by gamma-secretase and reduction in Abeta (show APP Antibodies) production.
secondary mutations in presenilin 1 (show PSEN1 Antibodies) alone activated the gamma-secretase activity.
Data indicate that familial Alzheimer's disease (FAD (show BRCA2 Antibodies)) 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 (show IL11RA Antibodies) induces processing of its C-terminal fragments by the gamma-secretase and the proteasome.
the G206D mutation reduced presenilin-1 (show PSEN1 Antibodies)-presenilin enhancer 2 interaction, but did not abolish gamma-secretase formation and presenilin-1 (show PSEN1 Antibodies) 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 (show PSEN1 Antibodies) endoproteolysis, allowing time for full assembly and proper trafficking.
Pen-2, as well as nicastrin (show NCSTN Antibodies) and Aph-1alpha (show APH1A Antibodies), is dispensable for presenilin endoproteolysis
Nct (show NCSTN Antibodies) has a critical role in the stability and proper intracellular trafficking of other components of the PS1 (show PSEN1 Antibodies)/ gamma-secretase complex but not in maintaining the association of PEN-2, APH-1 (show APH1A Antibodies), and full-length PS1 (show PSEN1 Antibodies)
APH-1 (show APH1A Antibodies) 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 (show NCSTN Antibodies), APH-1 (show APH1A Antibodies), 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