
HSP70/HSC70 | Heat shock prote
in 70- 询价
- Agrisera
- 瑞典
- AS09 592
- 2025年11月13日
- 1 : 10 000 (WB)
- Rabbit
- Arabidopsis thaliana, Acanthamoeba castellanii (amoeba), Caenorhabditis elegans, salmon (Salmo salar), Dictyostelium discoideum, frog-heart, Frog-skeletal muscle, Frog-liver, rainbow trout (Oncorhynchus mykiss), cow, Chicken, pig, Rat, seal, mummichog
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- 详细信息
- 文献和实验
- 技术资料
- 免疫原:
KLH-conjugated C-terminal synthetic peptide conserved in hsc/hsp70 sequences from a wide range of animal species
- 形态:
Lyophilized
- 保存条件:
Store lyophilized/reconstituted at -20°C; once rec
- 克隆性:
Polyclonal
- 标记物:
Chandra et al. (2012). Sustained high temperature increases the vitellogenin response to 17 alpha-ethynylestradiol in mummichog (Fundulus heteroclitus). Aquatic toxicology.
- 适应物种:
Arabidopsis thaliana, Acanthamoeba castellanii (amoeba), Caenorhabditis elegans, salmon (Salmo salar), Dictyostelium discoideum, frog-heart, Frog-skeletal muscle, Frog-liver, rainbow trout (Oncorhynchus mykiss), cow, Chicken, pig, Rat, seal, mummichog
- 级别:
分子生物学级
- 供应商:
Agrisera
- 宿主:
Rabbit
- 应用范围:
1 : 10 000 (WB)
- 靶点:
Heat-shock protein 70 (Hsp70) is the major stress-inducible protein in vertebrates and highly conserved throughout evolution. It plays a role as a molecular chaperone and is important for allowing cells to cope with acute stressor insult, especially those
- 抗体名:
HSP70/HSC70 | Heat shock protein 70
- 规格:
200 µl
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文献和实验Preparation of a Heat-Shock Protein 70-Based Vaccine from DCTumor Fusion Cells
We have developed an enhanced molecular chaperone-based vaccine through rapid isolation of heat-shock protein 70 peptide complexes (Hsp70.PC) after the fusion of tumor and dendritic cells (DCs) (Hsp70.PC-F). In this approach, the tumor
Isolation of Heat Shock Protein Complexes
Heat shock proteins (Hsp) are molecular chaperones with the capability to interact with a wide range of other proteins and are thus often found coupled with other heat shock and non-heat shock proteins. This can be an advantage to study
指将生物的整体、组织、细胞等从其生活的温度范围内急剧地从低温移向高温时,可显著地促进合成的一组蛋白质。例如将果蝇的幼虫或培养细胞从28℃移至 35℃时,则几乎大部分的蛋白质合成停止;与此相反,而休克蛋白的合成却反而被促进。这种促进作用主要是在转录 DNA的合成(转录)阶段产生的。同样的现象也见于哺乳类动物、培养细胞、原生动物、植物组织和细菌等。另外观察到,由休克以外的其他处理也会发生类似的现象。这种现象的生理意义尚不清楚,但推测是与生物的温度适应现象有关系。
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