Hsp70 高灵敏度 ELISA Kit-试剂盒-抗体-生物在线
Hsp70 高灵敏度 ELISA Kit

Hsp70 高灵敏度 ELISA Kit

商家询价

产品名称: Hsp70 高灵敏度 ELISA Kit

英文名称: Hsp70 High-Sensitivity ELISA Kit

产品编号: SKT-108

产品价格: null

产品产地: 加拿大

品牌商标: StressMarq

更新时间: null

使用范围: ELISA 样本类型 serum, plasma, cell lysates, tissue samples

StressMarq
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  • 地址 : 加拿大
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  • 电话 : 138****6620;
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  • 邮箱 : hedyl@stressmarq.com


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.

1. Zho, J. (1998) Cell. 94: 471-480.
2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol. 38 (1) 1-17.
3. Rothman J. (1989) Cell 59: 591 -601.
4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887.
5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2):869-876.
8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11):6200-6207.
9. Fernandez-Funez et al., (2000) Nature. 408(6808):101-106.

最新发表文献

1. Chichester, L., Wylie, A.T., Craft, S., Kavanagh, K. (2014). Muscle Heat Shock Protein 70 Predicts Insulin Resistance With Aging. J Gerontol A Biol Sci Med Sci. doi:10.1093/gerona/glu015