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Hsp70-Hsp90 Organizing Protein (HOP, p60) is an ~60kDa protein that is a critical intermediate component for the efficient maturation of steroid receptor complexes, serving to recruit Hsp90 to Hsp70-containing complexes. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a, and TPR2b.
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HSPs (heat shock proteins), HOP (hsp70-hsp90 organizing protein), and HIP (hsp70 interacting protein) protein expressions of liver tissue. (a) Bands, each line represents a repetition of each birds; (b) protein expressions level calculated by GAPDH. C, control; CH, chronic heat-stressed broiler; HH, early and chronic heat-stressed broiler. a,b Different superscript letters are significantly different (p < 0.05).
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Heat Treatment at an Early Age Has Effects on the Resistance to Chronic Heat Stress on Broilers. Animals (Basel) (2019)
LRET assays of the interactions of TPR mutants of HOP with HSP70 and HSP90. (A) Sequence alignment of the relevant portions of the TPR of CHIP and of TPR1 and TPR2A of HOP; K30 of CHIP, which is known to be important for binding HSP70 and HSP9032,33, is highlighted with a blue arrow. (B) Immunoblot analysis of TPR point mutants; HA-tagged constructs were transiently expressed in HEK293T cells and revealed using both anti-HOP and anti-HA antibodies as indicated with GAPDH as loading control. (C) Co-immunoprecipitation experiments to check the association between HOP mutants and endogenous HSP70 and HSP90; IP, immunoprecipitation; co-IP, coimmunoprecipitation; IB, immunoblot with indicated antibody. The uncropped original images of the immunoblots shown in panels B and C are presented in Supplementary Fig. S2. (D) Luminescence patterns of Tb3+ bound wild-type (LBT-TPR2A WT) and point mutant (LBT-TPR2A K229A). (E) Intrinsic EGFP fluorescence and LRET profiles for wild-type (WT) and point mutant TPR2A. (F) LRET titration experiment comparing the binding of wild-type and mutant TPR2A to HSP90. TPR2A WT and K229A (10 μM) loaded with equimolar Tb3+ were titrated with increasing concentrations of EGFP-C90 (0–6 μM). The Scatchard plot of the normalized LRET from three independent experiments represents means ± SEM. (G) Intrinsic TagRFP fluorescence and LRET profiles for wild-type (WT) and point mutant TPR1. In some panels, the position of the LRET signal is indicated.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes. Sci Rep (2018)
| Regulatory Status |
RUO – Research Use Only |
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Related Products
| Application | ELISA, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Mouse |