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Recombinant Human HSP70 (native, endotoxin-free)
Recombinant Human HSP70 (native, endotoxin-free)
- 中文名称：
- Recombinant Human HSP70 (native, endotoxin-free)
- 英文名称：
- Recombinant Human HSP70 (native, endotoxin-free)
- 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：
- AAA103774
- 规格：
- 0.05 mg|0.1 mg|2x0.1 mg
- 保存建议：
- Store at -20 degree C. Avoid freeze/ thaw cycle.
- 货期：
- 6-8周
- 纯度：
- Endotoxin-free, Multi-Step Purified
- 产品形式：
- 50mM Tris/HCI pH7.5, 2.5mM Bme, 0.l5M NaCl, 10% glycerol
- 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：
Scientific Background: Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (2). The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.
