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HSP90 alpha/beta 抗体 (AA 291-304) (FITC)

HSP90 alpha/beta 适用: 人 WB, ELISA, IHC, IF, ICC 宿主: 小鼠 Monoclonal Hyb-K41220A FITC
产品编号 ABIN2481319
发货至: 中国
  • 抗原 See all HSP90 alpha/beta products
    HSP90 alpha/beta (Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta))
    抗原表位
    • 11
    • 10
    • 2
    • 1
    • 1
    • 1
    AA 291-304
    适用
    • 41
    • 34
    • 33
    • 7
    • 6
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    宿主
    • 21
    • 16
    • 4
    小鼠
    克隆类型
    • 24
    • 16
    单克隆
    标记
    • 13
    • 4
    • 4
    • 4
    • 4
    • 3
    • 2
    • 2
    • 2
    • 2
    • 1
    This HSP90 alpha/beta antibody is conjugated to FITC
    应用范围
    • 41
    • 36
    • 14
    • 7
    • 6
    • 5
    • 3
    • 3
    Western Blotting (WB), ELISA, Immunohistochemistry (IHC), Immunofluorescence (IF), Immunocytochemistry (ICC)
    特异性
    Detects 90 kDa. Will detect both alpha (inducible) and beta (constitutively-expressed) forms.
    交叉反应
    人, 小鼠, 大鼠, Saccharomyces cerevisiae
    纯化方法
    Protein G Purified
    免疫原
    Recombinant human HSP90alpha, Specificity mapped to amino acids 291-304
    克隆位点
    Hyb-K41220A
    亚型
    IgG2a
  • 应用备注
    • WB (1:1000)
    • IHC (1:100)
    • ICC/IF (1:100)
    • optimal dilutions for assays should be determined by the user.
    说明

    1 μg/ml was sufficient for detection of HSP90αβ in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

    限制
    仅限研究用
  • 状态
    Liquid
    浓度
    1 mg/mL
    缓冲液
    PBS pH 7.2, 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
    4 °C
    储存方法
    Conjugated antibodies should be stored at 4°C
  • 抗原
    HSP90 alpha/beta (Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta))
    别名
    HSP90 alpha/beta (HSP90 alpha/beta 产品)
    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 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 (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.
    基因ID
    3326, 3320
    NCBI登录号
    NP_031381, NP_001017963
    UniProt
    P08238, P07900
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