HSP70 Antibody: Biotin-单抗-深圳欣博盛生物科技有限公司

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HSP70 Antibody: Biotin

品牌：Stressmarq

官网链接

说明书

折扣/货期

货号：SMC-230D-BI

规格：100 µg

目录价：￥4649.4

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:

HSP70 Antibody: Biotin

别名:

HSP70Bb Antibody, Heat Shock Protein 70Bb Antibody, dHSP70 Antibody, HSP70b Antibody, HSP70B Antibody, Dm-HSP70 Antibody

产品描述:

Rat Anti-Drosophila HSP70 Monoclonal IgG2B

反应种属:

Fruit Fly (Drosophila melanogaster)

宿主来源:

Rat

实验应用:

WB | ICC/IF | ELISA

靶标/特异性:

Detects ~70kDa (heat-inducible form).

同种型:

IgG2B

推荐稀释度:

WB (1:2000); optimal dilutions for assays should be determined by the user.

免疫原:

Prepared from Drosophila tissue culture cells heat shocked at 36.5◦C for 3 hours, and isolated using SDS PAGE.

免疫原种属:

Drosophila

克隆性:

Monoclonal

克隆号:

7FB

纯化方式:

Protein G Purified

偶联:

Biotin

产品浓度:

1 mg/ml

保存温度:

Conjugated antibodies should be stored according to the product label

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

Accession #:

NP_524927.2

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