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HSP90 抗体

HSP90 适用: 人 WB, IP, IHC, ELISA, IF, ICC 宿主: 兔 Polyclonal unconjugated
产品编号 ABIN361823
发货至: 中国
  • 抗原 See all HSP90 抗体
    HSP90 (Heat Shock Protein 90 (HSP90))
    适用
    • 119
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    宿主
    • 96
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    克隆类型
    • 99
    • 66
    多克隆
    标记
    • 56
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    This HSP90 antibody is un-conjugated
    应用范围
    • 136
    • 102
    • 90
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    Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)
    特异性
    Detects ~90 kDa.
    交叉反应
    人, 小鼠, 大鼠
    纯化方法
    Protein A Purified
    免疫原
    Full length protein HSP90
    Top Product
    Discover our top product HSP90 Primary Antibody
  • 应用备注
    • WB (1:500)
    • IHC (1:100)
    • ICC/IF (1:100)
    • optimal dilutions for assays should be determined by the user.
    说明

    A 1:500 dilution of ABIN361822 was sufficient for detection of 0.2 mg of purified HSP90 by ECL immunoblot analysis.

    限制
    仅限研究用
  • 状态
    Liquid
    浓度
    1 mg/mL
    缓冲液
    PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
    储存液
    Sodium azide
    注意事项
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    储存条件
    -20 °C
    储存方法
    -20°C
  • Bacci, Aiello, Ripoli, Loria, Pugliese, Pierconti, Rotili, Strigari, Pinto, Bassi, Mai, Grassi, Pontecorvi, Falcioni, Farsetti, Nanni: "H19-Dependent Transcriptional Regulation of β3 and β4 Integrins Upon Estrogen and Hypoxia Favors Metastatic Potential in Prostate Cancer." in: International journal of molecular sciences, Vol. 20, Issue 16, (2019) (PubMed).

    Re, Colussi, Nanni, Aiello, Bacci, Grassi, Pontecorvi, Farsetti: "Nucleoporin 153 regulates estrogen-dependent nuclear translocation of endothelial nitric oxide synthase and estrogen receptor beta in prostate cancer." in: Oncotarget, Vol. 9, Issue 46, pp. 27985-27997, (2018) (PubMed).

    Zhang, Pruitt, Tran, Du Bois, Zhang, Patel, Hoover, Simpson, Simmons, Gary, Snapper, Casellas, Mock: "B cell-specific deficiencies in mTOR limit humoral immune responses." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 191, Issue 4, pp. 1692-703, (2013) (PubMed).

    Verheyen, Peeraer, Nuydens, Dhondt, Poesen, Pintelon, Daniels, Timmermans, Meert, Carmeliet, Lambrechts: "Systemic anti-vascular endothelial growth factor therapies induce a painful sensory neuropathy." in: Brain : a journal of neurology, Vol. 135, Issue Pt 9, pp. 2629-41, (2012) (PubMed).

    Wagatsuma, Shiozuka, Kotake, Takayuki, Yusuke, Mabuchi, Matsuda, Yamada: "Pharmacological inhibition of HSP90 activity negatively modulates myogenic differentiation and cell survival in C2C12 cells." in: Molecular and cellular biochemistry, Vol. 358, Issue 1-2, pp. 265-80, (2011) (PubMed).

  • 抗原
    HSP90 (Heat Shock Protein 90 (HSP90))
    别名
    HSP90 (HSP90 产品)
    背景
    HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its 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 (5-6). 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 (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
    基因ID
    3326
    NCBI登录号
    NP_031381
    UniProt
    P08238
    途径
    M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
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