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- StressMarq
- 加拿大
- SPR-122
- 2025年11月23日
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- 保存条件：
-20ºC
- 保质期：
一年
- 英文名：
HSP90 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 | HSP90 蛋白 |
| 产品描述 |
重组恶性疟原虫HSP90部分蛋白 |
| 应用范围 | WB, SDS-PAGE |
| 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 | 恶性疟原虫 |
| 表达系统 | 大肠杆菌 (E. coli) |
| 氨基酸序列 | QPVLEINPNHFIIKQLNHLIQIDKMNLQNSEIAEQIFDVASMQGGYTIDDTGLFAKRVIGMMEKNAEQYLMNVQSNISNNTLNNNTSGSEMPQNNSPNELQSEMKSTNGIDDNSNISENKINESSSNQNNIGENSIAEENNIKNIAESDVNKINLGENDVSQNTMHKQDSGLFNLDPSILNSNMLSGSDKTLL |
| 纯度 | >90% |
| 蛋白长度 | 部分蛋白 |
产品特性
| 储存缓冲液 | 50mM Tris/HCl pH7.5, 300mM NaCl, 10% 甘油 |
| 储存温度 | -20ºC |
| 运输温度 | 蓝冰或4℃ |
| 纯化方式 | 亲和纯化的 |
| Protein Size | 分子量约为21.4 kD |
| 引用该产品 | P. Falciparum Recombinant HSP90 Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-122) |
| 分析证书 | 该蛋白已经通过SDS-PAGE检测证明纯度大于90%. |
生物学特性
| 别名 | PfHsp90 Protein, Pf14_-417 HSP90 Protein, Hsp90 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 | 细胞核, 细胞质 |
| Accession Number | XP_001348591.1 |
| GeneID | 811999 |
| Swiss Prot | Q8IL32 |
| 科研背景 | HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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 immune adsorption 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 (9). Recently, Prof. Tatu’s laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. Falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide |
| 参考资料 | 1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y., et al. (1991) J.Biol Chem. 266: 10099-10103. 3. Arlander S.J.H, et al. (2003) J Biol Chem. 278: 52572-52577. 4. Pearl H., et al. (2001) Adv Protein Chem. 59: 157-186. 5. Neckers L., et al. (2002) Trends Mol Med. 8: S55-S61. 6. Pratt W., Toft D. (2003) Exp Biol Med. 228: 111-133. 7. Pratt W., Toft D. (1997) Endocr Rev. 18: 306–360. 8. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420–434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 8324–8328. 10. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278(20): 18336-45. 11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279(45): 46692-9. |
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，如乙胺嘧啶，可起病因预防作用。 （2）红细胞内期：原发性红细胞外期在肝细胞内生成的大量裂殖子破坏肝细胞而进入血液，侵入红细胞，经滋养体发育成裂殖体，并破坏红细胞，释放出大量裂殖子及其代谢产物，再加上红细胞破坏产生的大量变性蛋白，至一定程度，刺激机体，引起寒战、高热等症状。从红细胞内逸出的裂殖子又复进入红细胞进行发育。如此周而复始，每完成一个无性生殖周期，引起一次症状发作。不同种的疟原虫完成无性生殖周期所需时间不同：恶性疟36～48小时，间日疟48小时，三日疟72小时。对此期疟原虫有杀灭作用
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，加上它在温度低于恶性疟原虫的情况下在蚊子中繁殖的能力，使它的分布能够延伸到温带气候。间日疟占亚洲和南美洲疟疾病例的65%，但在非洲大陆的大部分地区却没有。红细胞入侵间日疟原虫和恶性疟原虫的另一个主要区别是疟原虫入侵的红细胞类型。经历这种入侵的寄生虫的阶段是分生子。入侵是一个多阶段的过程，由识别和附着，红细胞膜。这之后是定位和形成一个紧密的连接之间的寄生虫和宿主膜入侵前。间日疟原虫的分生子并不利用成熟的红细胞，而是优先侵入未成熟的红细胞，即网织红细胞。与网状细胞表面的连接是通过其表面的一种被称为达菲
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重组恶性疟原虫HSP90部分蛋白
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