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生物来源
rabbit
质量水平
抗体形式
purified immunoglobulin
抗体产品类型
primary antibodies
克隆
polyclonal
种属反应性
human, rat, mouse
制造商/商品名称
Chemicon®
技术
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
NCBI登记号
UniProt登记号
运输
wet ice
靶向翻译后修饰
unmodified
基因信息
human ... HSP90AA1(3320)
mouse ... Hsp90Aa1(15519)
rat ... Hsp90Aa1(299331)
特异性
Reacts with a protein of 84 kD identified as heat shock protein 90beta (HSP90beta). No reactivity with HSP90alpha/HSP86.
CELLULAR LOCALIZATION: Nuclear and Cytoplasmic.
CELLULAR LOCALIZATION: Nuclear and Cytoplasmic.
免疫原
Synthetic peptide corresponding to amino acids 2-13 from the N-terminus of mouse heat shock protein 90b.
应用
Immunoblotting: 5 μg/mL
Immunohistochemistry (frozen and formalin/paraffin): 5-10 μg/mL. Staining of formalin fixed tissue sections requires boiling the tissue sections in 10mM citrate buffer, pH 6.0 for 10-20 minutes followed by cooling at room temperature for 20 minutes.
Immunocytochemistry
Immunoprecpitation: 10 μg/mg of protein lysate.
Optimal working dilutions must be determined by end user.
Immunohistochemistry (frozen and formalin/paraffin): 5-10 μg/mL. Staining of formalin fixed tissue sections requires boiling the tissue sections in 10mM citrate buffer, pH 6.0 for 10-20 minutes followed by cooling at room temperature for 20 minutes.
Immunocytochemistry
Immunoprecpitation: 10 μg/mg of protein lysate.
Optimal working dilutions must be determined by end user.
Research Category
Protein Trafficking
Protein Trafficking
Research Sub Category
Chaperones
Chaperones
This Anti-Heat Shock Protein 90β Antibody is validated for use in IP, WB, IC, IH(P) for the detection of Heat Shock Protein 90β.
外形
Format: Purified
Purified immunoglobulin. Liquid in 10 mM PBS, pH 7.4 with 0.2% BSA and 15 mM sodium azide.
储存及稳定性
Maintain at 2-8°C in undiluted aliquots for up to 6 months.
分析说明
Control
POSITIVE CONTROL: MAD109 cells or breast carcinoma.
POSITIVE CONTROL: MAD109 cells or breast carcinoma.
其他说明
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
法律信息
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
免责声明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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储存分类代码
12 - Non Combustible Liquids
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Thorsten Stühmer et al.
British journal of haematology, 147(3), 319-327 (2009-08-19)
The 90 kD heat shock protein (Hsp90) molecular chaperone sustains multiple components of oncogenic pathways and has recently emerged as a therapeutic target that is now being clinically tested in a number of malignancies. In order to address formulation issues
Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVP-AUY922 in multiple myeloma.
Stuhmer, T; Zollinger, A; Siegmund, D; Chatterjee, M; Grella, E; Knop, S; Kortum et al.
Leukemia null
Ying-Li Wu et al.
Journal of cell science, 119(Pt 13), 2797-2806 (2006-06-15)
The involvement of telomerase in cellular immortalization and senescence has often been assessed by means of telomerase expression at the RNA level and quantification of telomerase activity by the telomeric repeat amplification protocol assay. However, these methods either neglected the
Vrushali Sagare-Patil et al.
Journal of assisted reproduction and genetics, 34(4), 495-503 (2017-02-27)
The aims of this paper were to study whether heat shock protein 90 (HSP90) is a regulator of sperm functions and to determine its association with oligoasthenozoospermia. The levels of HSP90 in sperm lysates were measured by ELISA. Localization of
Tanja Heimberger et al.
British journal of haematology, 160(4), 465-476 (2012-12-21)
The heat shock transcription factor 1 (HSF1) has recently been reported to promote malignant transformation and growth. Here we provide experimental evidence for a role of HSF1 in the pathogenesis of multiple myeloma (MM). Immunohistochemical analyses revealed that HSF1 was
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