Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.
规格 | 价格/CNY | 货期 | 数量 | |
---|---|---|---|---|
100 μg | ¥ 4,460 | 5日内发货 | ||
1 mg | ¥ 29,000 | 5日内发货 |
生物活性 | Testing in progress |
产品描述 | Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development. |
种属 | Mouse |
表达系统 | Baculovirus-Insect Cells |
标签 | His |
蛋白编号 | NP_032328.2 |
别名 | AL024080, Hspca, hsp4, Hsp86-1, heat shock protein 90kDa α (cytosolic), class A member 1, 86kDa, Hsp90, AL024147, heat shock protein 90kDa alpha (cytosolic), class A member 1, 89kDa, Hsp89, Hsp90 α |
蛋白构建 | A DNA sequence encoding the Mouse HSP90AA1 (NP_032328.2) (Met1-Asp733) was expressed, with a polyhistidine tag at the N-terminus. |
蛋白纯度 | ≥ 95 % as determined by SDS-PAGE. |
分子量 | 87.19 kDa (predicted) |
内毒素 | < 1.0 EU per μg protein as determined by the LAL method. |
缓冲液 | Lyophilized from sterile 20mM PB, 300mM NaCl, 10% glycerol, 1mM TCEP, 0. 5mM PMSF, pH 7.0. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA. |
复溶方法 | A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
存储 |
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
运输方式 |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
研究背景 | Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development. |
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HSP90 alpha Protein, Mouse, Recombinant (His) AL024080 Hspca hsp4 Hsp86-1 heat shock protein 90kDa α (cytosolic), class A member 1 AL-024080 86kDa Hsp90 AL024147 AL-024147 heat shock protein 90kDa alpha (cytosolic), class A member 1 89kDa AL 024147 Hsp89 Hsp90 α AL 024080 recombinant recombinant-proteins proteins protein