Prion Protein + Cdk5/p25 Lysate
€179.00
In stock
SKU
ECM-PL7401
Background:
Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of 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. 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. Human recombinant Prion protein includes the full length protein along with an N-terminal GST fusion protein. This Prion protein was phosphorylated with active Cdk5/p25 in an in vitro kinase assay. The phosphorylated Prion protein is detected by anti-Prion Protein (a.a. 109-112) (Cat.#PM3971) and anti-Prion Protein (Ser-43) (Cat.#PP3951).
Buffer/Storage:
Prion recombinant protein lysate is supplied at a concentration of 5 ng/µl in electrophoresis sample buffer (62.5 mM Tris pH 6.8, 2% SDS, 5% glycerol, 0.003% bromophenol blue, 0.9% β-mercaptoethanol). Store at –20°C. Do not boil or dilute. Stable for 1 year.
Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of 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. 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. Human recombinant Prion protein includes the full length protein along with an N-terminal GST fusion protein. This Prion protein was phosphorylated with active Cdk5/p25 in an in vitro kinase assay. The phosphorylated Prion protein is detected by anti-Prion Protein (a.a. 109-112) (Cat.#PM3971) and anti-Prion Protein (Ser-43) (Cat.#PP3951).
Buffer/Storage:
Prion recombinant protein lysate is supplied at a concentration of 5 ng/µl in electrophoresis sample buffer (62.5 mM Tris pH 6.8, 2% SDS, 5% glycerol, 0.003% bromophenol blue, 0.9% β-mercaptoethanol). Store at –20°C. Do not boil or dilute. Stable for 1 year.
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