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Rabbit polyclonal anti hsp 90a b

Manufactured by Santa Cruz Biotechnology
Sourced in United States

Rabbit polyclonal anti-HSP-90α/β is a laboratory reagent used to detect and quantify the expression of the Heat Shock Protein 90 (HSP-90) in biological samples. HSP-90 is a highly conserved molecular chaperone that plays a crucial role in the folding, stability, and function of various client proteins.

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2 protocols using rabbit polyclonal anti hsp 90a b

1

Analysis of XPO1-p53 Interaction by Western Blot

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Western blot analysis was performed as described previously (24 (link)). The following antibodies were used: mouse monoclonal anti-p53 (DO-1; Santa Cruz Biotechnology, Santa Cruz, CA, USA); rabbit polyclonal anti-XPO1 (Santa Cruz Biotechnology); rabbit polyclonal anti-HSP-90a/b (Santa Cruz Biotechnology); rabbit monoclonal histone H3 (Cell Signaling Technologies, Beverly, MA, USA); rabbit monoclonal GAPDH (Cell Signaling Technologies); and mouse monoclonal anti-β-actin (Sigma Chemical Co., St Louis, MO, USA). Nuclear and cytoplasmic proteins were extracted using a subcellular fractionation kit (ProteoExtract; EMD Millipore Corporation, Billerica, MA, USA), according to the manufacturer's protocol. Protein lysates were also subjected to immunoprecipitation using anti-XPO1 and immunoprecipitates were subjected to western blot analysis with anti-XPO1 or p53. Visualized blots were analyzed by the MultiGauge 3.1 software (Fujifilm, Tokyo, Japan).
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2

Western Blot Analysis of Protein Localization

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Western blot analysis was carried out as described previously.(24 (link)) The following antibodies were used: mouse monoclonal anti-p53 (DO-1; Santa Cruz Biotechnology, Santa Cruz, CA, USA); rabbit polyclonal anti-XPO1 (Santa Cruz Biotechnology); rabbit polyclonal anti-HSP-90a/b (Santa Cruz Biotechnology); rabbit monoclonal histone H3 (Cell Signaling Technologies, Beverly, MA, USA); rabbit monoclonal GAPDH (Cell Signaling Technologies); and mouse monoclonal anti-β-actin (Sigma Chemical Co., St Louis, MO, USA). Nuclear and cytoplasmic proteins were extracted using a subcellular fractionation kit (ProteoExtract; EMD Millipore, Billerica, MA, USA), according to the manufacturer's protocol. Protein lysates were also subjected to immunoprecipitation using anti-XPO1 and immunoprecipitates were subjected to Western blot analysis with anti-XPO1 or p53. Visualized blots were analyzed by the MultiGauge 3.1 software (Fujifilm, Tokyo, Japan).
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