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HSP90 alpha Protein, Human, Recombinant (His)

HSP90 alpha Protein, Human, Recombinant (His)

产品编号 TMPY-06845
别名: EL52, HSP89A, heat shock protein 90kDa alpha (cytosolic), class A member 1, HSPN, HSPCAL4, HSPCA, HSP90N, heat shock protein 90kDa α (cytosolic), class A member 1, HSPCAL1, Hsp90 α, HSPC1, LAP2, Hsp89, LAP-2, HSP86, Hsp90, HSP90A

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, Human, Recombinant (His)
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
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产品目录号及名称: HSP90 alpha Protein, Human, Recombinant (His) (TMPY-06845)
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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 Human
表达系统 Baculovirus-Insect Cells
标签 His
蛋白编号 NP_005339.3
别名 EL52, HSP89A, heat shock protein 90kDa alpha (cytosolic), class A member 1, HSPN, HSPCAL4, HSPCA, HSP90N, heat shock protein 90kDa α (cytosolic), class A member 1, HSPCAL1, Hsp90 α, HSPC1, LAP2, Hsp89, LAP-2, HSP86, Hsp90, HSP90A
蛋白构建 A DNA sequence encoding the Human HSP90AA1 (NP_005339.3) (Met1-Asp732) was expressed, with a polyhistidine tag at the N-terminus.
蛋白纯度 ≥ 90 % as determined by SDS-PAGE.
分子量 87.06 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, 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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Keywords

HSP90 alpha Protein, Human, Recombinant (His) EL52 HSP89A heat shock protein 90kDa alpha (cytosolic), class A member 1 HSPCAL 4 HSPN HSPC-1 HSPCAL4 HSPCA HSPCAL-4 HSP90N heat shock protein 90kDa α (cytosolic), class A member 1 HSPCAL1 LAP 2 HSPCAL-1 Hsp90 α HSPC1 HSP-86 HSPCAL 1 EL 52 LAP2 Hsp89 EL-52 LAP-2 HSP 86 HSP86 Hsp90 HSPC 1 HSP90A recombinant recombinant-proteins proteins protein

 

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