Rqn1 (C-Term) 抗体
适用: Saccharomyces cerevisiae
WB
宿主: 兔
Polyclonal
unconjugated
1 image
(3 references)-
- 抗原
- Rqn1
- 抗原表位
- C-Term
- 适用
- Saccharomyces cerevisiae
- 宿主
- 兔
- 克隆类型
- 多克隆
- 应用范围
- Western Blotting (WB)
- 交叉反应 （详细）
- Not tested in other species.
- 产品特性
- Rabbit polyclonal antibody affinity purified with the synthetic peptide used as antigen
- 纯化方法
- Affinity purified
- 免疫原
- Synthetic peptide CSQQNNNGNQNRY corresponding to the C-terminus region of Rnq1
- 亚型
- IgG
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- 应用备注
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1) Western blotting: 300 fold dilution.
Not tested for other applications. - 限制
- 仅限研究用
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- 状态
- Liquid
- 缓冲液
- PBS, 1 mg/mL BSA, 0.09 % sodium azide, 50 % glycerol
- 储存液
- Sodium azide
- 注意事项
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- 储存条件
- -20 °C/-80 °C
- 储存方法
- -20 C (For long term storage: -70 C)
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: "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).
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: "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).
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- 抗原
- Rqn1
- 背景
- 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.
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