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- 详细信息
- 文献和实验
- 技术资料
- 免疫原:
Recombinant Human Heat shock 70 kDa protein 1-like protein (420-641AA)
- 亚型:
IgG
- 形态:
Liquid
- 保存条件:
Upon receipt, store at -20℃ or -80℃. Avoid repeated freeze.
- 克隆性:
Polyclonal
- 标记物:
Non-conjugated
- 适应物种:
Human
- 保质期:
6个月
- 抗原来源:
Homo sapiens (Human)
- 目录编号:
P34931
- 级别:
优
- 库存:
200
- 供应商:
武汉华美生物工程有限公司
- 宿主:
Rabbit
- 应用范围:
ELISA, WB, IHC, IF; Recommended dilution: WB:1:1000-1:5000, IHC:1:20-1:200, IF:1:50-1:200
- 浓度:
>95%,Protein G purified
- 靶点:
HSPA1L
- 抗体英文名:
HSPA1L Antibody
- 抗体名:
Spermatid specific heat shock protein 70 antibody
- 规格:
100μl/50μl/20μl
| 规格: | 100μl | 产品价格: | ¥1320.0 |
|---|---|---|---|
| 规格: | 50μl | 产品价格: | ¥880.0 |
| 规格: | 20μl | 产品价格: | ¥440.0 |
保存缓冲液
Preservative: 0.03% Proclin 300Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
功能
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365). Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810).风险提示:丁香通仅作为第三方平台,为商家信息发布提供平台空间。用户咨询产品时请注意保护个人信息及财产安全,合理判断,谨慎选购商品,商家和用户对交易行为负责。对于医疗器械类产品,请先查证核实企业经营资质和医疗器械产品注册证情况。
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
Immunization of mice, with preparations of heat shock proteins (HSPs) isolated from tumors or virus-infected cells, has been shown to elicit specific protective immunity against the tumor or the virus-infected cells used as the source
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