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HSP70 Antibody

品牌：Stressmarq

官网链接

说明书

折扣/货期

货号：SMC-100B

规格：200 µg

目录价：￥4485.6

产品详情

产品名称:

HSP70 Antibody

别名:

HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody

产品描述:

Mouse Anti-Human HSP70 Monoclonal IgG1

反应种属:

宿主来源:

Mouse

实验应用:

WB | IHC | ICC/IF | ELISA | FCM | FACS | IEM | Bl | AM

靶标/特异性:

Detects ~70kDa. Does not cross-react with HSC70 (HSP73).

同种型:

IgG1

免疫原:

Human HSP70

免疫原种属:

Human

克隆性:

Monoclonal

克隆号:

C92F3A-5

纯化方式:

Protein G Purified

偶联:

Unconjugated

产品浓度:

1 mg/ml

保存温度:

-20ºC

运输温度:

Blue Ice or 4ºC

存储溶液:

PBS pH7.4, 50% glycerol, 0.1% sodium azide *Storage buffer may change when conjugated

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 44 kDa 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 locations, 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. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.

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