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| 规格： | 50ul | 产品价格： | ￥1180.0 |
|---|---|---|---|
| 规格： | 100ul | 产品价格： | ￥1980.0 |
| 规格： | 200ul | 产品价格： | ￥2800.0 |
| 产品编号 | bs-16560R |
| 英文名称 | Hsp104 Rabbit pAb |
| 中文名称 | 热休克蛋白104抗体 |
| 英文别名 | L0948; Heat shock protein 104; HS104_YEAST; Hsp 104. |
| 产品应用 | IHC-P=1:100-500, IHC-F=1:100-500, ICC/IF=1:100-500, IF=1:100-500, ELISA=1:5000-10000 Not yet tested in other applications. |
| 交叉反应 | (Human, Mouse, Saccharomyces cerevisiae) |
| 抗体来源 | Rabbit |
| 免疫原 | KLH conjugated synthetic peptide derived from YEAST Hsp104 |
| 亚型 | IgG |
| 性状 | Liquid |
| 纯化方法 | affinity purified by Protein A |
| 克隆类型 | Polyclonal |
| 理论分子量 | 102 kDa |
| 浓度 | 1mg/ml |
| 储存液 | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| 研究领域 | Signal Transduction > Protein Trafficking > Chaperones > Heat Shock Proteins |
| 亚基 | Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity at NBD2. Interacts with YDJ1. Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7 and STI1 (via TPR repeats); under respiratory growth conditions. |
| 亚细胞定位 | Cytoplasmic and Nuclear |
| 相似性 | Belongs to the ClpA/ClpB family. |
| 功能 | Hsp104 is a molecular chaperone required for stress tolerance and for maintenance of [psi(+)] prions in the budding yeast Saccharomyces cerevisiae. Hsp104 is vital to protect yeast cells against high temperature and high concentration of ethanol. It is not required for normal growth. |
| 保存条件 | Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | Hsp104 is a molecular chaperone required for stress tolerance and for maintenance of [psi(+)] prions in the budding yeast Saccharomyces cerevisiae (1,2). HSP104 is a hexameric protein with two AAA ATPase domains (N- and C-terminal nucleotide-binding domains NBD1 and NBD2, respectively) per monomer (3). NBD1 and NBD2 have very different catalytic properties, but each shows positive cooperativity in hydrolysis (3,4). Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo (5). Hsp104 interacts with Hsp90 cochaperones in respiring yeast (1). The primary function of Hsp104 in prion propagation is to disassemble prion aggregates and generate the small prion seeds that initiate new rounds of prion propagation (possibly assisted by Hsp70-Ssa) (6). |
| 应用 | 推荐稀释比例 |
| {IHC-P} | {1:100-500} |
| {IHC-F} | {1:100-500} |
| {ICC/IF} | {1:100-500} |
| {IF} | {1:100-500} |
| {ELISA} | {1:5000-10000} |
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文献和实验Nucleic Acid Programmable Protein Arrays: Versatile Tools for Array‐Based Functional Protein Studies
Blass, S., Engel, J.M., and Burmester, G.R., 1999. The immunologic homunculus in rheumatoid arthritis. Arthritis Rheum. 42:2499‐2506.
Models and Analysis of Atherosclerosis, Restenosis, and Aneurysm Formation in the Mouse
., Plump, A.S., Raines, E.W., Breslow, J.L., and Ross, R. 1994. ApoE‐deficient mice develop lesions of all phases of atherosclerosis throughout the arterial tree. Arterioscler. Thromb. Vasc. Biol. 14:133‐140.
Generation of Spatio‐Temporally Controlled Targeted Somatic Mutations in the Mouse
during formation of the lung. Proc. Natl. Acad. Sci. U.S.A. 99:10482‐10487. Rajewsky, K., Gu, H., Kuhn, R., Betz, U. A., Muller, W., Roes, J., and Schwenk, F. 1996. Conditional gene
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