Rqn1 (C-Term) antibody
-
- Target
- Rqn1
- Binding Specificity
- C-Term
- Reactivity
- Saccharomyces cerevisiae
- Host
- Rabbit
- Clonality
- Polyclonal
- Application
- Western Blotting (WB)
- Cross-Reactivity (Details)
- Not tested in other species.
- Characteristics
- Rabbit polyclonal antibody affinity purified with the synthetic peptide used as antigen
- Purification
- Affinity purified
- Immunogen
- Synthetic peptide CSQQNNNGNQNRY corresponding to the C-terminus region of Rnq1
- Isotype
- IgG
-
- Application Notes
-
1) Western blotting: 300 fold dilution.
Not tested for other applications. - Restrictions
- For Research Use only
-
- Format
- Liquid
- Buffer
- PBS, 1 mg/mL BSA, 0.09 % sodium azide, 50 % glycerol
- Preservative
- Sodium azide
- Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Storage
- -20 °C/-80 °C
- Storage Comment
- -20 C (For long term storage: -70 C)
-
-
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." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 35, pp. 12934-9, (2004) (PubMed).
: "The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions." in: Genes to cells : devoted to molecular & cellular mechanisms, Vol. 9, Issue 8, pp. 685-96, (2004) (PubMed).
: "Rnq1: an epigenetic modifier of protein function in yeast." in: Molecular cell, Vol. 5, Issue 1, pp. 163-72, (2000) (PubMed).
: "
-
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." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 35, pp. 12934-9, (2004) (PubMed).
-
- Target
- Rqn1
- Background
- 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.
-