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HSP70 Protein, Mouse, Recombinant (His Tag)
HSP70 Protein, Mouse, Recombinant (His Tag)
- 中文名称：
- HSP70 Protein, Mouse, Recombinant (His Tag)
- 英文名称：
- HSP70 Protein, Mouse, Recombinant (His Tag)
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA258246
- 规格：
- 0.1 mg|2x0.1 mg|3x0.1 mg|4x0.1 mg|5x0.1 mg
- 保存建议：
- Samples are stable for twelve months from date of receipt at -20 degree C to -80 degree C
Store it under sterile conditions at -20 degree C to -80 degree C upon receiving. Recommend to aliquot the protein into smaller quantities for optimal storage.
Avoid repeated freeze-thaw cycles.
- 货期：
- 6-8周
- 纯度：
- > 95% as determined by SDS-PAGE.
> 90% as determined by SEC-HPLC
- 产品形式：
- Lyophilized from sterile PBS, pH 7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP is synthesized intracellularly, which may protect cells from protein denaturation or death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates the presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulate their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release.
