Rqn1 (C-Term) antibody

Catalog No. ABIN2452117

This Rabbit Polyclonal antibody specifically detects Rqn1 in WB. It exhibits reactivity toward Saccharomyces cerevisiae. It has been mentioned in 3+ publications

Quick Overview for Rqn1 (C-Term) antibody (ABIN2452117)

Target: Rqn1

Reactivity: Saccharomyces cerevisiae

Host: Rabbit

Clonality: Polyclonal

Application: Western Blotting (WB)

Product Details

Binding Specificity: C-Term

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 Details

Application Notes: 1) Western blotting: 300 fold dilution.
Not tested for other applications.

Restrictions: For Research Use only

Handling

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)

References

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." in: 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." in: 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." in: Molecular cell, Vol. 5, Issue 1, pp. 163-72, (2000) (PubMed).

Target Details

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.