产品简要
公司名称 :
StressMarq Biosciences
产品类型 :
抗体
产品名称 :
HSP90抗体
目录 :
SMC-107B
规格 :
200微克
价格 :
314.00美元
克隆性 :
单克隆
宿主 :
小鼠
共轭标签 :
未共轭
克隆名称 :
H9010
反应物种 :
人类, 小鼠, 大鼠, 犬
应用 :
免疫印迹, 酶联免疫吸附测定, 免疫组化, 免疫细胞化学, 免疫沉淀
更多信息或购买 :
StressMarq Biosciences 产品网页
文章摘录数: 20
出版应用/物种/样本/稀释参考文献
  • 免疫印迹; 人类; 图 5b, 6c
Inda M, Joshi S, Wang T, Bolaender A, Gandu S, Koren Iii J, et al. The epichaperome is a mediator of toxic hippocampal stress and leads to protein connectivity-based dysfunction. Nat Commun. 2020;11:319 pubmed 出版商
  • 免疫组化; 人类; 1:500; 图 3b
Rodina A, Wang T, Yan P, Gomes E, Dunphy M, Pillarsetty N, et al. The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature. 2016;538:397-401 pubmed 出版商
  • 免疫印迹; 人类; 图 1
Dong H, Zou M, Bhatia A, Jayaprakash P, Hofman F, YING Q, et al. Breast Cancer MDA-MB-231 Cells Use Secreted Heat Shock Protein-90alpha (Hsp90α) to Survive a Hostile Hypoxic Environment. Sci Rep. 2016;6:20605 pubmed 出版商
  • 免疫印迹; 人类
Hunter M, O Hagan K, Kenyon A, Dhanani K, Prinsloo E, Edkins A. Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. PLoS ONE. 2014;9:e86842 pubmed 出版商
  • 免疫印迹; 人类; 1:2500
Patel P, Yan P, Seidler P, Patel H, Sun W, Yang C, et al. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. Nat Chem Biol. 2013;9:677-84 pubmed 出版商
  • 免疫印迹; 人类; 1:2000
Taldone T, Zatorska D, Patel P, Zong H, Rodina A, Ahn J, et al. Design, synthesis, and evaluation of small molecule Hsp90 probes. Bioorg Med Chem. 2011;19:2603-14 pubmed 出版商
  • 免疫印迹; 人类; 1:4000
Gershburg S, Murphy L, Marschall M, Gershburg E. Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization. Biochem J. 2010;431:227-35 pubmed 出版商
Peksel B, Gombos I, Peter M, Tiszlavicz Á, Brameshuber M, Balogh G, et al. Mild heat induces a distinct "eustress" response in Chinese Hamster Ovary cells but does not induce heat shock protein synthesis. Sci Rep. 2017;7:15643 pubmed 出版商
Guo J, Jayaprakash P, Dan J, Wise P, Jang G, Liang C, et al. PRAS40 Connects Microenvironmental Stress Signaling to Exosome-Mediated Secretion. Mol Cell Biol. 2017;37: pubmed 出版商
Dong H, Le Y, Wang Y, Zhao H, Huang C, Hu Y, et al. Extracellular heat shock protein 90? mediates HDM-induced bronchial epithelial barrier dysfunction by activating RhoA/MLC signaling. Respir Res. 2017;18:111 pubmed 出版商
de la Mare J, Jurgens T, Edkins A. Extracellular Hsp90 and TGFβ regulate adhesion, migration and anchorage independent growth in a paired colon cancer cell line model. BMC Cancer. 2017;17:202 pubmed 出版商
Zou M, Bhatia A, Dong H, Jayaprakash P, Guo J, Sahu D, et al. Evolutionarily conserved dual lysine motif determines the non-chaperone function of secreted Hsp90alpha in tumour progression. Oncogene. 2017;36:2160-2171 pubmed 出版商
Matsuzaka Y, Tanihata J, Komaki H, Ishiyama A, Oya Y, Ruegg U, et al. Characterization and Functional Analysis of Extracellular Vesicles and Muscle-Abundant miRNAs (miR-1, miR-133a, and miR-206) in C2C12 Myocytes and mdx Mice. PLoS ONE. 2016;11:e0167811 pubmed 出版商
Tunnah L, MacKellar S, Barnett D, MacCormack T, Stehfest K, Morash A, et al. Physiological responses to hypersalinity correspond to nursery ground usage in two inshore shark species (Mustelus antarcticus and Galeorhinus galeus). J Exp Biol. 2016;219:2028-38 pubmed 出版商
Goldstein R, Yang S, Taldone T, Chang B, Gerecitano J, Elenitoba Johnson K, et al. Pharmacoproteomics identifies combinatorial therapy targets for diffuse large B cell lymphoma. J Clin Invest. 2015;125:4559-71 pubmed 出版商
Teigen L, Orczewska J, McLaughlin J, O Brien K. Cold acclimation increases levels of some heat shock protein and sirtuin isoforms in threespine stickleback. Comp Biochem Physiol A Mol Integr Physiol. 2015;188:139-47 pubmed 出版商
Jayaprakash P, Dong H, Zou M, Bhatia A, O Brien K, Chen M, et al. Hsp90α and Hsp90β together operate a hypoxia and nutrient paucity stress-response mechanism during wound healing. J Cell Sci. 2015;128:1475-80 pubmed 出版商
Bessemer R, Butler K, Tunnah L, Callaghan N, Rundle A, Currie S, et al. Cardiorespiratory toxicity of environmentally relevant zinc oxide nanoparticles in the freshwater fish Catostomus commersonii. Nanotoxicology. 2015;9:861-70 pubmed 出版商
Espallergues J, Teegarden S, Veerakumar A, Boulden J, Challis C, Jochems J, et al. HDAC6 regulates glucocorticoid receptor signaling in serotonin pathways with critical impact on stress resilience. J Neurosci. 2012;32:4400-16 pubmed 出版商
Chen Q, Prior M, Dargusch R, Roberts A, Riek R, Eichmann C, et al. A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease. PLoS ONE. 2011;6:e27865 pubmed 出版商
产品信息
目录号 :
SMC-107B
产品名称 :
HSP90抗体
描述 :
小鼠抗人类HSP90单克隆IgG2a
靶标 :
HSP90
共轭标签 :
未共轭
2021标价 :
314.00美元
Currency :
美元
研究领域(s) :
Cancer Heat Shock Cell Signaling Protein Trafficking Chaperone Proteins Cancer Tumor Biomarkers
别称(s) :
HSP84抗体, HSP90抗体, HSP90乙抗体, HSP90B抗体, HSPC2抗体, HSPCB抗体
规格 :
200微克
类别 :
抗体
产品类型 :
单克隆
克隆编号 :
H9010
免疫原 :
重组人类HSP90beta
免疫原物种 :
人类
登录号 :
NP_031381.2
Swiss Prot数据库 :
P08238
应用 :
免疫印迹免疫组化免疫细胞化学/IF免疫沉淀酶联免疫吸附测定艾姆斯氏试验
宿主物种 :
小鼠
抗体亚型 :
IgG2a
物种活性缩写 :
Hu Ms Rt Rb Ck Dg Fs Shk Hm
物种活性全称 :
Human Mouse Rat Rabbit Chicken Dog Fish White Sucker Fish (Catostomus commersonii) Shark Gummy Shark (Mustelus antarcticus) School Shark (Galeorhinus galeus) Hamster
抗体稀释 :
WB (1:2500), IHC (1:100); optimal dilutions for assays should be determined by the user.
纯化 :
蛋白质G纯化
储存缓冲液 :
PBS pH7.2, 50% 甘油, 0.09% 叠氮化钠
浓度 :
1毫克/毫升
特异性 :
Detects 90kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.
储存温度 :
-20ºC
运输温度 :
Blue Ice or 4ºC
Cite this Product :
StressMarq Biosciences Cat# SMC-107B, RRID: AB_854214
化验分析证明书 :
1 µg/ml of SMC-107 was sufficient for detection of HSP90beta in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Cellular Localization :
细胞质黑素体
科研背景 :
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
参考文献 :
1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y., et al. (1991), J.Biol Chem. 266: 10099-10103. 3. Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577. 4. Pearl H., et al. (2001) Adv Protein Chem 59:157-186. 5. Neckers L., et al. (2002) Trends Mol Med 8:S55-S61. 6. Pratt W., Toft D. (2003) Exp Biol Med 228:111-133. 7. Pratt W., Toft D. (1997) Endocr Rev 18:306–360. 8. Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328. 10. Barent R. L. (1998) Mol. Endocrinol. 12: 342-354 11. Lo. M.A. (1998) EMBO J. 17: 6879-6887.
Field of Use :
Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
Image Filenames :
SMC-107_Hsp90_Antibody_H9010_IHC_Human_colon-carcinoma_40x_1.png SMC-107_Hsp90_Antibody_H9010_WB_Human_cell-lysates-from-various-cell-lines_1.png SMC-107_Hsp90_Antibody_H9010_IHC_Human_colon-carcinoma_40x_2.png SMC-107_Hsp90_Antibody_H9010_IHC_Mouse_inflamed-colon_40x_2.png SMC-107_Hsp90_Antibody_H9010_IHC_Mouse_backskin_1.png SMC-107_Hsp90_Antibody_H9010_WB_Human_HeLa-cell-lysates_1.png SMC-107_Hsp90_Antibody_H9010_WB_Human_Lysates_1.png
SMC-107_Hsp90_Antibody_H9010_IHC_Mouse_
inflamed-colon_40x_1.png
更多信息或购买 :
StressMarq Biosciences 产品网页
公司信息
StressMarq Biosciences
PO Box 55036 CADBORO BAY
3825 Cadboro Bay Road
Victoria BC V8N 4G0
info@stressmarq.com
http://www.stressmarq.com
1-250-294-9065
公司总部: 加拿大
StressMarq Biosciences Inc.是由Dr.Louwrier创建与温哥华的维多利亚，专注于热休克、细胞压力、离子通道及细胞信号研究领域，提供大量经过严格验证的抗体、蛋白及试剂盒。公司致力于提供高质量试剂以满足并超越客户期望。它也推出抗体试用项目，特别针对于新的研究领域，鼓励客户在购买之前先测试小规格试用产品。此外，公司提供采用新专利免疫组化技术的试剂盒，采用前所未有的抗体浓度进行实验。