| 货号:SPR-101A | 规格:50 µg | 目录价:¥1776.6 |
产品详情
* 以下信息仅供参考,详情请以原厂网站为准
产品名称:
Human Recombinant HSP90 alpha Protein
别名:
HSP86 Protein, HSP89A Protein, HSP90A Protein, HSP90AA1 Protein, HSPC1 Protein, HSPCA Protein, HSPCAL3 Protein, HSP90alpha Protein
产品描述:
Human Recombinant HSP90 alpha Protein
反应种属:
Human
实验应用:
WB | SDS-PAGE | ATPase Activity Assay | Surface Plasmon Resonance (SPR) | DARTs Assay (Drug Affinity Responsive Target Stability Assay) | SB (Skin Blotting)
纯化方式:
Affinity Purified
偶联:
No tag
产品浓度:
Lot/batch specific. See included datasheet.
表达系统:
E. coli
保存温度:
-20ºC
运输温度:
Blue Ice or 4ºC
预期分子量:
~90 kDa
存储溶液:
50mM Tris/HCl pH7.5, 5mM Bme, 0.3M NaCl, 10% glycerol
产地:
加拿大
功能与背景:
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 at http://www.HSP90.ca.
纯度:
>90%
Accession #:
NP_001017963.2
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