Human Recombinant HSP70 Full Length Protein-其他重组蛋白-深圳欣博盛生物科技有限公司

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Human Recombinant HSP70 Full Length Protein

品牌：Stressmarq

官网链接

说明书

折扣/货期

货号：SPR-117B

规格：100 µg

目录价：￥6652.8

产品详情

* 以下信息仅供参考，详情请以原厂网站为准

产品名称:

Human Recombinant HSP70 Full Length Protein

别名:

HSP70 1 Protein, HSP70 2 Protein, HSP70.1 Protein, HSP72 Protein, HSP73 Protein, HSPA1 Protein, HSPA1A Protein, HSPA1B Protein

产品描述:

Human Recombinant HSP70 Full Length Protein

反应种属:

Human

实验应用:

WB | SDS-PAGE | ATPase Activity Assay | Functional Assay | ELISA

纯化方式:

Multi-Step Purified | Endotoxin-free

偶联:

No tag

产品浓度:

Lot/batch specific. See included datasheet.

表达系统:

Baculovirus/Sf9 cells

保存温度:

-20ºC

运输温度:

Blue Ice or 4ºC

预期分子量:

~70 kDa

存储溶液:

50mM Tris/HCl pH7.5, 0.3M NaCl, 10% glycerol, 0.1mM EDTA

产地:

加拿大

功能与背景:

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 50% 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

纯度:

>90%

Accession #:

M11717

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