Prion Protein (phospho-Ser-43) Blocking Peptide
€155.00
In stock
SKU
ECM-PX3955
Background:
Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of normal cellular prion protein (PrPc) into a form that is insoluble and resistant to proteases (PrPSc). The protease resistant form can polymerize into fibrils which accumulate in infected tissues and cause cell death and tissue damage. PrPs have an N-terminal signal sequence and a C-terminal linkage to glycosylphosphatidylinositol anchor. The mature protein is a glycosylated protein that associates with cell membranes. Phosphorylation of PrPC at Ser-43 by Cdk5 promotes proteinase K resistance, prion aggregation, and fibril formation in vitro. In addition, Ser-43 phosphorylation is upregulated in scrapie-infected mouse brain relative to controls. Thus, phosphorylation of Ser-43 may be an important mechanism leading conversion of PrPc to PrPSc and the onset of disease.
Sequence: Phospho-Prion Protein (Ser-43) peptide includes amino acids surrounding serine 43 in human prion protein. This sequence has high homology to the conserved site in rat, mouse, and bovine prion protein.
Specificity: The peptide is specifically recognized by anti-Prion Protein (Ser-43) antibody (PP3951) in ELISA, and has been shown to block the reactivity of PP3951 during Western blot. In addition, the peptide is recommended for use in blocking PP3951 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of normal cellular prion protein (PrPc) into a form that is insoluble and resistant to proteases (PrPSc). The protease resistant form can polymerize into fibrils which accumulate in infected tissues and cause cell death and tissue damage. PrPs have an N-terminal signal sequence and a C-terminal linkage to glycosylphosphatidylinositol anchor. The mature protein is a glycosylated protein that associates with cell membranes. Phosphorylation of PrPC at Ser-43 by Cdk5 promotes proteinase K resistance, prion aggregation, and fibril formation in vitro. In addition, Ser-43 phosphorylation is upregulated in scrapie-infected mouse brain relative to controls. Thus, phosphorylation of Ser-43 may be an important mechanism leading conversion of PrPc to PrPSc and the onset of disease.
Sequence: Phospho-Prion Protein (Ser-43) peptide includes amino acids surrounding serine 43 in human prion protein. This sequence has high homology to the conserved site in rat, mouse, and bovine prion protein.
Specificity: The peptide is specifically recognized by anti-Prion Protein (Ser-43) antibody (PP3951) in ELISA, and has been shown to block the reactivity of PP3951 during Western blot. In addition, the peptide is recommended for use in blocking PP3951 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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