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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
-20ºC
- 保质期:
一年
- 英文名:
HSP60 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 | HSP60 蛋白 |
| 产品描述 |
活性重组人HSP60蛋白 |
| 应用范围 | WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA |
| 浓度 | 各批次不同,请详见说明书 |
| 标记物 | His 标签 |
| 性质 | 重组 |
| 来源物种 | 人 |
| 表达系统 | 大肠杆菌 (E. coli) |
| 纯度 | >90% |
| Full Biological Activity | ATPase 活性 |
产品特性
| 储存缓冲液 | 20mM 磷酸缓冲液, 150mM 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60kD |
| 引用该产品 | Human Recombinant HSP60 Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-104) |
| 分析证书 | 该蛋白已经通过SDS-PAGE检测证明纯度大于90%. 此蛋白出厂时的ATP酶活性为每小时从每微克蛋白质分离出3.6μM 磷酸根 (使用孔雀绿磷酸检测, 200μl反应液, 20ul的1mM ATP, 37°C, pH7.5 ). |
| 其他相关信息 | 具有ATP酶活性 |
生物学特性
| 别名 | 60kDa chaperonin Protein, cb863 Protein, CPN60 Protein, GROEL Protein, GroEL Homolog Protein, HLD4 Protein, Hsp65 Protein, HSPD1 Protein, HuCHA60 Protein, SPG13 Protein |
| 研究领域 | 伴侣蛋白, 标签和细胞标记物, 热休克, 癌症, 细胞信号传导, 细胞器标记物, 蛋白质运输 |
| 细胞定位 | 细胞核, 细胞质, 黑素体 |
| Accession Number | BC003030 |
| GeneID | 3329 |
| Swiss Prot | P10809 |
| 科研背景 | In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many different species. The common characteristics of the HSP60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, HSP60 with its co-chaperonin, HSP10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of HSP60-HSP10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9). |
| 参考资料 | 1. Hartl F.U. (1996) Nature. 381: 571-579. 2. Bukau B. and Horwich A.L. (1998) Cell. 92: 351-366. 3.Hartl F.U. and Hayer-Hartl M. (2002) Science. 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biol. 9: 2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7.Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris C.C. et al. (2006) Cell Stress Chaperones. 11: 116-128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297. |
产品图片

60kDa Hsp60 蛋白 SDS-PAGE (SPR-104).
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文献和实验[1] Dieudé M, Correa J A, Neville C, et al. Association of autoantibodies to heat‐shock protein 60 with arterial vascular events in patients with antiphospholipid antibodies[J]. Arthritis & Rheumatism, 2011, 63(8): 2416-2424.
[2] Werner C, Stangl S, Salvermoser L, et al. Hsp70 in liquid biopsies—A tumor-specific biomarker for detection and response monitoring in cancer[J]. Cancers, 2021, 13(15): 3706.
[3] Hu F, Guo Q, Wei M, et al. Chlorogenic acid alleviates acetaminophen-induced liver injury in mice via regulating Nrf2-mediated HSP60-initiated liver inflammation[J]. European Journal of Pharmacology, 2020, 883: 173286.
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