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Rafoxanide

Cat. No. M8885
Rafoxanide Structure
Size Price Availability Quantity
200mg USD 150  USD150 In stock
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Quality Control & Documentation
Biological Activity

Rafoxanide is a novel allosteric inhibitor of SPAK and OSR1. Rafoxanide is also a salicylanilide used as an anthelmintic.

In vitro kinase assays using Rafoxanide showed it to be a low micromolar inhibitor of OSR1 T185E in vitro, IC50 = 8.18 μM. Rafoxanide is also a low micromolar inhibitor of SPAK T233E in vitro with IC50 value of 13.03 μM.

Protocol (for reference only)
Cell Experiment
Cell lines HEK293 cells
Preparation method HEK293 cells were first treated with Rafoxanide or Closantel at the indicated concentrations or STOCK1S5 0699 (10 μM) for 30 min and then either left untreated or treated with hypotonic buffer for 30 min to activate WNK-SPAK/OSR1 signalling. The cells were then harvested, and the lysates were probed for phospho-NKCC1 T203, T207 and T212, total NKCC1, phospho-SPAKS373, total SPAK and GAPDH as a loading control.
Concentrations 1, 3, 10, 20, 50 μM
Incubation time 30 min
Animal Experiment
Animal models
Formulation
Dosages
Administration
Chemical Information
Molecular Weight 626.01
Formula C19H11Cl2I2NO3
CAS Number 22662-39-1
Solubility (25°C) DMSO: ≥ 60 mg/mL
Storage Powder          -20°C   3 years ;  4°C   2 years
In solvent       -80°C   6 months ;  -20°C   1 month
Conversion of different model animals based on BSA (PMID: 27057123)
Species Mouse Rat Rabbit Guinea pig Hamster Dog
Weight (kg) 0.02 0.15 1.8 0.4 0.08 10
Body Surface Area (m2) 0.007 0.025 0.15 0.05 0.02 0.5
Km factor 3 6 12 8 5 20
Animal A (mg/kg) = Animal B (mg/kg) multiplied by  Animal B Km
Animal A Km

For example, to modify the dose of Compound A used for a mouse (20 mg/kg) to a dose based on the BSA for a rat, multiply 20 mg/kg by the Km factor for a mouse and then divide by the Km factor for a rat. This calculation results in a rat equivalent dose for Compound A of 10 mg/kg.

References

[1] AlAmri MA, et al. ChemMedChem. Rafoxanide and Closantel Inhibit SPAK and OSR1 Kinases by Binding to a Highly Conserved Allosteric Site on Their C-terminal Domains.

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