HSP70/HSPA1 Mouse mAb  (货号:B12954)

说明书

货号:B12954

规格价格
50ul ¥1080.00 加购物车
100ul ¥2050.00 加购物车
反应 Human,Mouse
宿主 Mouse
克隆性 Monoclonal
预测反应 WB: HeLa , Homo sapiens
应用 WB
推荐浓度 WB: 1:2000 - 1:5000
理论分子量 70kDa
实测分子量 70kDa
形式 Liquid
保存条件 Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3.
偶联物 Unconjugated
阳性对照 HepG2,HeLa,A-549,293T,mouse brain
细胞定位 blood microparticle,centriole,centrosome,cytoplasm,cytosol,endoplasmic reticulum,extracellular exosome,extracellular region,focal adhesion,mitochondrion,nuclear speck,nucleoplasm,nucleus,perinuclear region of cytoplasm,plasma membrane
纯化 Affinity purification

相关产品

查找相关产品 >>

抗原信息

抗原信息 Recombinant fusion protein.
序列 Email For Sequence

靶点信息

研究背景 This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins.
基因ID 3303
基因名
Swiss P0DMV8
别名 HSPA1A;HEL-S-103;HSP70-1;HSP70-1A;HSP70.1;HSP70I;HSP72;HSPA1;HSP70
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 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 (PubMed:24012426, PubMed:26865365, PubMed:24318877). 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 (PubMed:27708256). 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 (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).
研究领域

实验步骤

实验步骤

文献引用

暂无数据

客户评价

未选文件 允许的格式:jpg,png 每张图片最大1M,支持多选

HSP70/HSPA1 Mouse mAb 有 0 条评价