HSP90AB1 抗体 (AA 185-335)
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- 抗原 See all HSP90AB1 抗体
- HSP90AB1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1))
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抗原表位
- AA 185-335
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适用
- 人
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宿主
- 小鼠
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克隆类型
- 单克隆
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标记
- This HSP90AB1 antibody is un-conjugated
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应用范围
- Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunoprecipitation (IP)
- 特异性
- Detects 90 kDa. This is a beta specific product, does not cross-react with alpha isoforms.
- 交叉反应
- 人, 小鼠
- 纯化方法
- Protein G Purified
- 免疫原
- Recombinant human HSP90beta, Specificity mapped to amino acids 185-335
- 克隆位点
- Hyb-K3701
- 亚型
- IgM
- Top Product
- Discover our top product HSP90AB1 Primary Antibody
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- 应用备注
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- WB (1:1000)
- IHC (1:3000)
- optimal dilutions for assays should be determined by the user.
- 说明
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1 μg/ml was sufficient for detection of HSP90β 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
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- 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
- -20 °C
- 储存方法
- -20°C
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Moderate alcohol induces stress proteins HSF1 and hsp70 and inhibits proinflammatory cytokines resulting in endotoxin tolerance." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 4, pp. 1975-87, (2014) (PubMed).
: "Extensive gene-specific translational reprogramming in a model of B cell differentiation and Abl-dependent transformation." in: PLoS ONE, Vol. 7, Issue 5, pp. e37108, (2012) (PubMed).
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Moderate alcohol induces stress proteins HSF1 and hsp70 and inhibits proinflammatory cytokines resulting in endotoxin tolerance." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 4, pp. 1975-87, (2014) (PubMed).
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- 抗原
- HSP90AB1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1))
- 别名
- HSP90 beta (HSP90AB1 产品)
- 别名
- D6S182 antibody, HSP84 antibody, HSP90B antibody, HSPC2 antibody, HSPCB antibody, GRP94 antibody, TRA1 antibody, hsp90b antibody, 90kDa antibody, AL022974 antibody, C81438 antibody, Hsp84 antibody, Hsp84-1 antibody, Hsp90 antibody, Hspcb antibody, Hsp70 antibody, Hsp70-1 antibody, Hsp70.1 antibody, hsp68 antibody, HSP90-BETA antibody, hsp90beta antibody, wu:fa29f01 antibody, wu:fa91e11 antibody, wu:fd59e11 antibody, wu:gcd22h07 antibody, HSP90 antibody, heat shock protein 90 alpha family class B member 1 antibody, heat shock protein 90 beta family member 1 antibody, Heat Shock Protein 90, endoplasmic reticulum antibody, heat shock protein 90B antibody, heat shock protein 90 alpha (cytosolic), class B member 1 antibody, heat shock protein 1B antibody, heat shock protein 90kDa alpha family class B member 1 S homeolog antibody, heat shock protein 90, alpha (cytosolic), class B member 1 antibody, HSP90AB1 antibody, HSP90B1 antibody, HSP90B antibody, hsp90ab1 antibody, Hsp90ab1 antibody, Hspa1b antibody, hsp90ab1.S antibody
- 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
- NCBI登录号
- NP_031381
- UniProt
- P08238
- 途径
- Regulation of Cell Size
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