相关产品推荐更多 >
万千商家帮你免费找货
0 人在求购买到急需产品
- 详细信息
- 文献和实验
- 技术资料
- 免疫原:
A synthetic peptide of human HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B
- 亚型:
IgG
- 保存条件:
Store at -20℃. Avoid freeze/thaw cycles.
- 克隆性:
Polyclonal Antibody
- 标记物:
Biotin,Cy3,Cy3.5,Cy5,Cy5.5,Cy7,FITC,HRP,RBITC,Solar Fluor 350,Solar Fluor 405,Solar Fluor 488,Solar Fluor 532,Solar Fluor 555,Solar Fluor 568,Solar Fluor 594,Solar Fluor 633,Solar Fluor 640,Solar Fluor 647,Solar Fluor 660,Solar Fluor 680,Solar Fluor 750
- 适应物种:
Human;Rat;Mouse
- 抗原来源:
A synthetic peptide of human HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B
- 目录编号:
3305/3303/3304
- 级别:
实验级别
- 库存:
现询
- 供应商:
北京索莱宝科技有限公司
- 宿主:
Rabbit
- 应用范围:
WB
- 浓度:
WB 1:1000-3000.
- 靶点:
HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B
- 抗体英文名:
Anti-HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B Polyclonal Antibody
- 抗体名:
HSP70-Hom;HSP70-1;HSP70.1;HSP72;HSPA1;HSX70;HSP70-2;HSP70.2;HSP72
- 规格:
20ul/100ul/50ul
| 规格: | 20ul | 产品价格: | ¥480.0 |
|---|---|---|---|
| 规格: | 100ul | 产品价格: | ¥1600.0 |
| 规格: | 50ul | 产品价格: | ¥960.0 |
| 基本信息 | |
| 英文名称 | Anti-HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B Polyclonal Antibody |
| 宿主 | Rabbit |
| 克隆类型 | Polyclonal Antibody |
| 亚型 | IgG |
| 交叉反应 | Human;Rat;Mouse |
| 预测交叉反应 | Cow(100%);Pig(100%);Monkey(100%);Fish(85.7%) |
| 应用 | WB |
| 稀释比例 | WB 1:1000-3000. |
| 密度 | |
| 靶标 | HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B |
| 别名 | HSP70-Hom;HSP70-1;HSP70.1;HSP72;HSPA1;HSX70;HSP70-2;HSP70.2;HSP72 |
| 背景说明 | 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. Positive regulator of PRKN translocation to damaged mitochondria.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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. 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. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response.(Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. 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. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.(Microbial infection)In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. |
| Swiss Prot | P34931/P0DMV8/P0DMV9 |
| Gene ID | 3305/3303/3304 |
| 亚细胞定位 | Cytoplasm Nucleus |
| 免疫原 | A synthetic peptide of human HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B |
| Public Immunogen Range | 515-565/641aa |
| 理论分子量 | 70/64kDa |
| EC | |
| 纯化方法 | Affinity purification |
| 储存液 | PBS with 50% Glycerol,0.03% Proclin300,0.5% BSA,pH 7.3. |
| 储存条件 | Store at -20℃. Avoid freeze/thaw cycles. |
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。
文献和实验扫描仪中,都采用机械式的二维X,Y线性扫描技术实现,即X,Y方向都采用直线驱动器和直线导轨实现往复运动。此类装置,由于驱动系统的频率限制,驱动器的扫描惯性大,使得扫描效率低,分析时间相当长;并且往复行程长,对直线导轨的精度要求相当高。二、光机结合的二维扫描系统为同样实现生物芯片的二维扫描,我们的实验装置设计如图2,采用了振镜和大数值孔径的远心f-è物镜相结合实现X方向扫描,Y方向的运动仍采用直线驱动器和直线导轨实现。 系统中,对于f-è物镜,满足x=2fè(è为振镜的摆动角度,f为物镜焦距)的线性
() #交换 x 轴和 y 轴> p + ylim(0,15) #如果想截取某一段可以用此命令设置值域。> p + scale_x_continuous(breaks =seq(18,34,50) ) #设置刻度线位置> p + theme(axis.text.x = element_text(angle = 90,family = "Times",face = "italic",colour = "darkred",size=rel(0.9))) # angle = 90 设置字体角度, family
2:选择浸泡后加洗次数。F 2F1(01)浸泡后清洗一次,F2F1(10)浸泡后清洗二次,F2F1(11)浸泡后清洗三次。 F wet(湿)-F dry(干)选择板在最终洗完后是湿还是干。 2)旋钮功能: volume(液量):调节阀门的开启时间来调整洗液量1×50?滋l。 washes(清洗次数);设定浸泡前的洗板次数。 pause(暂停):设定洗板过程中的暂停时间(秒) soak(浸泡):设置洗板程序完成后的一段浸泡时间1×0.5min。 3. 注意事项
技术资料暂无技术资料 索取技术资料










