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- Leading Biology
- AMR12148N
- 美国
- 2026年03月31日
- Rabbit
- Human, Mouse, Rat
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- 详细信息
- 文献和实验
- 技术资料
- 靶点：
ASCR; AltPrP; CD230; CJD; GSS; KURU; PRIP; PrP; PrP27-30; PrP33-35C; PrPc; p27-30
- 浓度：
Affinity purification
- 宿主：
Rabbit
- 适应物种：
Human, Mouse, Rat
- 保质期：
1-2年
- 供应商：
安诺伦（北京）生物科技有限公司
- 保存条件：
Store at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.
- 形态：
形式：Liquid 储存溶液：Buffer: PBS with 0.02% sodium azide, 0.05% BSA, 50% glycerol, pH7.3.
- 亚型：
IgG
- 免疫原：
A synthesized peptide derived from human Prion Protein
- 规格：
50 µl/100 µl/200 µl
| 规格： | 50 µl | 产品价格： | ￥1650.0 |
|---|---|---|---|
| 规格： | 100 µl | 产品价格： | ￥2685.0 |
| 规格： | 200 µl | 产品价格： | ￥4230.0 |
Observed MW: 30KDa
细胞定位：Cell membrane, Cytoplasm, GPI-anchor, Golgi apparatus, Lipid-anchor, Nucleus
稀释方法：WB 1:500 - 1:2000
总结：The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2014]
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文献和实验Secondary structure of prion mRNA
carbohydrate-binding pro-tein 35 and other RNA-binding proteins. Neurodegen-eration, 3, 177189. Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L. & Prusiner, S. B. (1993). Structural analysis of the scrapie prion protein
A Bioinformatics Method for Identifying Q/N-Rich Prion-Like Domains in Proteins
Numerous proteins contain domains that are enriched in glutamine and asparagine residues, and aggregation of some of these proteins has been linked to both prion formation in yeast and a number of human diseases. Unfortunately
1. Materials(1) Antibody 7E3, 2L sup grown in flasks, frozen and thawed overnight.(2) BioRad Affi-Gel Protein A MAPS II Buffers cat. #1530-6160 ($161.00)(3) 50 mM Tris pH7.8.(4) 40 g ammonium sulfate for every 100 ml Sup.(5) 4L 100 mM Tris/pH
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