This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
-20 °C/-80 °C
Stockage commentaire
-20 C (For long term storage: -70 C)
Derkatch, Uptain, Outeiro, Krishnan, Lindquist, Liebman: "Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 35, pp. 12934-9, (2004) (PubMed).
Kimura, Koitabashi, Kakizuka, Fujita: "The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions." dans: Genes to cells : devoted to molecular & cellular mechanisms, Vol. 9, Issue 8, pp. 685-96, (2004) (PubMed).
Sondheimer, Lindquist: "Rnq1: an epigenetic modifier of protein function in yeast." dans: Molecular cell, Vol. 5, Issue 1, pp. 163-72, (2000) (PubMed).
Antigène
Rqn1
Sujet
Background: The glutamine- and asparagine-rich protein, Rnq1, is a putative yeast prion. Rnq1 protein with yet unknown function, can exists in either noninfectious soluble monomer form, [pin-], or the insoluble aggregated amyloid-like form called [PIN+]. The insoluble state is dominant and transmitted between cells through the cytoplasm. Rnq1 protein is necessary for the de novo induction of another prion, [PSI+]. The molecular chaperone Hsp104 is necessary for the aggregate formation of polyglutamine and for the maintenance of prion phenotype. The pre-existing aggregates are required for the chaperon-dependent establishment of the epigenetic trait in yeast prions.