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Description:
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Presenilin 1 belongs to the peptidase A22A family. Predicted molecular weight approximately 53 kD. Presenilins assemble with nicastrin, PEN-2, and APH-1 into an active g-secretase complex responsible for proteolytic cleavage of amyloid precursor protein (APP) and transmembrane cleavage of Notch receptor proteins. Presenilin 1 is subjected to an endoproteolytic cleavage, generating a stable heterodimer composed of an N-terminal and a C-terminal fragment. Presenilin 1 may play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane and involved in stimulates cell-cell adhesion, negatively regulating Wnt signaling, and hematopoiesis. Presenilin1 residues Ser353 and Ser357 are phosphorylated by GSK-3β. The Poly6366 antibody recognizes human phospho-Presenilin 1 (Ser353/Ser357) and has been shown to be useful for immunoflorence staining. This antibody does not detect Presenilin 1 phosphorylated at other sites. |
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Other Names:
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Presenilin 1, PS-1, Protein S182 |
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Structure:
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Belongs to the peptidase A22A family. Predicted molecular weight approximately 53 kD. |
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Distribution:
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Expressed in a wide range of tissues including various regions of the brain, liver, spleen and lymph nodes. |
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Function:
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May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Involved in stimulation of cell-cell adhesion, negatively regulating Wnt signaling, and hematopoiesis. |
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Interaction:
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Notch 1-4, Catenin alpha 1, Catenin beta, CDK5, Caspase 1, Bcl 2, MAPT, PKC?, Filamin A, Caspase 8, BCLX, Caspase 3, Caspase 6-8, Nicastrin, FBW7, APH1A, APH1B, PEN-2 |
Antigen
References:
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1. Laudon, H., et al. 2005. J. Biol. Chem. 280: 35352
2. De Strooper, B. 2003. Neuron 38: 9
3. Kirschenbaum F., et al. 2001. J. Biol. Chem. 276:7366 |
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