H90-10 single-chain antibody recognizes Hsp90beta by immunoprecipitation and Western blotting

Authors

  • Didier Picard University of Geneva
  • Ernest Abboud
  • Lilia Bernasconi

DOI:

https://doi.org/10.24450/journals/abrep.2021.e285

Keywords:

Molecular chaperone, Hsp90, Immunoblotting, Immunoprecipitation

Abstract

The recombinant antibody H90-10 detects the endogenous human heat-shock protein 90 beta (Hsp90β) by immunoprecipitation (IP) and Western blotting.

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References

Holt SE, Aisner DL, Baur J, et al. Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 1999; 13(7):817–26. PMID:10197982

Barent RL, Nair SC, Carr DC, et al. Analysis of FKBP51/FKBP52 Chimeras and Mutants for Hsp90 Binding and Association with Progesterone Receptor Complexes. Mol Endocrinol. 1998; 12(3):342–54. PMID:9514152

Bhattacharya K, Weidenauer L, Luengo TM, et al. The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation. Nat Commun. 2020; 11(1):5975. PMID:33239621

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Published

14-01-2021

How to Cite

1.
Picard D, Abboud E, Bernasconi L. H90-10 single-chain antibody recognizes Hsp90beta by immunoprecipitation and Western blotting. Antib. Rep. [Internet]. 2021Jan.14 [cited 2021Mar.2];4(1). Available from: https://oap.unige.ch/journals/abrep/article/view/285

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