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- 详细信息
- 询价记录
- 文献和实验
- 技术资料
- 保存条件:
-20ºC
- 保质期:
一年
- 英文名:
HSP90 beta Protein
- 库存:
大量
- 供应商:
StressMarq
- 规格:
50 µg/100 µg/100 µg x2
| 规格: | 50 µg | 产品价格: | 询价 |
|---|---|---|---|
| 规格: | 100 µg | 产品价格: | 询价 |
| 规格: | 100 µg x2 | 产品价格: | 询价 |
| 产品名称 | HSP90beta 蛋白 |
| 产品描述 |
活性重组人HSP90beta全长蛋白 |
| 应用范围 | WB, SDS-PAGE, Functional Assay, ELISA, Co-IP, SPR |
| 浓度 | 各批次不同,请详见说明书 |
| 标记物 | 无标签 |
| 性质 | 重组 |
| 来源物种 | 人 |
| 表达系统 | 杆状病毒/Sf9细胞 |
| 氨基酸序列 | MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD |
| 纯度 | >85% |
| 蛋白长度 | 全长蛋白 |
产品特性
| 储存缓冲液 | 20mM Tris, pH 7.5, 175 mM NaCl, 0.1 mM EDTA, 10% 甘油, 1 mM DTT |
| 储存温度 | -20ºC |
| 运输温度 | 蓝冰或4℃ |
| 纯化方式 | 低内毒素, 亲和纯化的 |
| Protein Size | 分子量约为90kD |
| 引用该产品 | Human Recombinant Human HSP90 beta Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-102) |
| 分析证书 | 该蛋白已经通过SDS-PAGE检测证明纯度大于90%. |
| 其他相关信息 | 原蛋白序列, 无内毒素 |
生物学特性
| 别名 | FLJ26984 Protein, Hsp84 Protein, Hsp90 Protein, Hsp90B Protein, HspC2 Protein, HspCB Protein |
| 研究领域 | 伴侣蛋白, 热休克, 癌症, 细胞信号传导, 蛋白质运输, 肿瘤标记物 |
| 细胞定位 | 细胞质, 黑素体 |
| Accession Number | NP_031381.2 |
| GeneID | 3326 |
| Swiss Prot | P08238 |
| 科研背景 | HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide. |
| 参考资料 | 1. Arlander S.J.H., et al. (2003) J Biol Chem. 278: 52572-52577. 2. Pearl H., et al. (2001) Adv Protein Chem. 59:157-186. 3. Neckers L., et al. (2002) Trends Mol Med. 8:S55-S61. 4. Pratt W., Toft D. (2003) Exp Biol Med. 228:111-133. 5. Pratt W., Toft D. (1997) Endocr Rev. 18: 306–360. 6. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420–434. 7. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 8324– 8328. |
产品图片

90kDa Hsp90 beta 蛋白SDS-PAGE (SPR-102). 泳道 1: 分子量梯 (MW). 泳道 2: 人HSP90 beta 蛋白 (SPR-101).
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文献和实验[1] Gaonkar R, Shiralgi Y, Lakkappa D B, et al. Essential oil from Cymbopogon flexuosus as the potential inhibitor for HSP90[J]. Toxicology reports, 2018, 5: 489-496.
[2] Goode K M, Petrov D P, Vickman R E, et al. Targeting the Hsp90 C-terminal domain to induce allosteric inhibition and selective client downregulation[J]. Biochimica et Biophysica Acta (BBA)-General Subjects, 2017, 1861(8): 1992-2006.
[3] Ding X, Meng C, Dong H, et al. Extracellular Hsp90α, which participates in vascular inflammation, is a novel serum predictor of atherosclerosis in type 2 diabetes[J]. BMJ Open Diabetes Research and Care, 2022, 10(1): e002579.
[4] Rozenberg P, Ziporen L, Gancz D, et al. Cooperation between Hsp90 and mortalin/GRP75 in resistance to cell death induced by complement C5b-9[J]. Cell death & disease, 2018, 9(2): 150.
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