Cat. No.: HY-N15205

Rhinacanthin C

Rhinacanthin C is an orally active naphthoquinone ester and P-gp inhibitor (IC₅₀ = 5.20 μM). Rhinacanthin C exerts effects in ameliorating hepatic steatosis, insulin resistance, and inflammation by inhibiting P-gp, BCRP, OATP1B1/1B3, and multiple CYP enzymes, downregulating lipid synthesis-related factors such as ACC and FAS, and upregulating AMPKα phosphorylation and SIRT1. Rhinacanthin C can be used in research on non-alcoholic fatty liver disease, diabetes, abnormal osteolysis, Alzheimer's disease, and inflammation.

For research use only. We do not sell to patients.

CAS No.: 159278-74-7
Formula: C₂₅H₃₀O₅
Molecular Weight:410.50

Storage:

Please store the product under the recommended conditions in the Certificate of Analysis.

Rhinacanthin C Chemical Structure

CAS No.: 159278-74-7

Price

Stock

Quantity

Amount: USD 0.00

* Please select Quantity before adding items.

Use of MCE Products

Strong Fluorescence Signal / Multi-Disciplinary Applications / High Fluorescence Specificity

Biological Activity
- Description
- IC₅₀ & Target
- Cellular Effect
- In Vitro
- In Vivo
Chemical Information
Protocols (9)
Purity & Documentation
References
Calculators
Help & FAQs
Classifications
Bioz

Biological Activity

Description

IC₅₀ & Target

^[5]^[1]

P-gp

5.20 μM (IC₅₀)

BCRP

0.83 μM (IC₅₀)

OATP1B1

OATP1B3

AMPKα

SIRT1

All AMPK Isoforms :

All Sirtuin Isoforms :

Cellular Effect

Cell Line	Type	Value	Description	References
Caco-2	IC50	5.20 μM	Inhibition of P-gp-mediated transport of digoxin across Caco-2 cell monolayers incubated for 180 mins with sampling every 30 mins by UHPLC-MS/MS analysis. Inhibition of P-gp-mediated transport of digoxin across Caco-2 cell monolayers incubated for 180 mins with sampling every 30 mins by UHPLC-MS/MS analysis.	31399508
MDCK-II	IC50	0.83 μM	Inhibition of BCRP-mediated transport of prazosin across MDCKII-BCRP cell monolayers incubated for 180 mins with sampling every 30 mins by UHPLC-MS/MS analysis. Inhibition of BCRP-mediated transport of prazosin across MDCKII-BCRP cell monolayers incubated for 180 mins with sampling every 30 mins by UHPLC-MS/MS analysis.	31399508
HEK293	IC50	0.70 μM	Inhibition of OATP1B1-mediated uptake of 8-FcA in HEK293-OATP1B1 cells pre-incubated for 30 mins followed by incubation with substrate for 10 mins measured by fluorescence at 485/535 nm. Inhibition of OATP1B1-mediated uptake of 8-FcA in HEK293-OATP1B1 cells pre-incubated for 30 mins followed by incubation with substrate for 10 mins measured by fluorescence at 485/535 nm.	31399508
HEK293	IC50	3.95 μM	Inhibition of OATP1B3-mediated uptake of 8-FcA in HEK293-OATP1B3 cells pre-incubated for 30 mins followed by incubation with substrate for 10 mins measured by fluorescence at 485/535 nm. Inhibition of OATP1B3-mediated uptake of 8-FcA in HEK293-OATP1B3 cells pre-incubated for 30 mins followed by incubation with substrate for 10 mins measured by fluorescence at 485/535 nm.	31399508
HeLa	IC50	26.2 μM	Antiproliferative activity against human cervical carcinoma HeLa cells assessed as reduction in cell viability incubated for 3 days at 37 °C by WST-1 colorimetric assay. Antiproliferative activity against human cervical carcinoma HeLa cells assessed as reduction in cell viability incubated for 3 days at 37 °C by WST-1 colorimetric assay.	23742857
PC-3	IC50	1.92 μM	Antiproliferative activity against human prostate carcinoma PC-3 cells assessed as reduction in cell viability incubated for 3 days at 37 °C by WST-1 colorimetric assay. Antiproliferative activity against human prostate carcinoma PC-3 cells assessed as reduction in cell viability incubated for 3 days at 37 °C by WST-1 colorimetric assay.	23742857
T-24	IC50	0.660 μM	Antiproliferative activity against human bladder carcinoma T24 cells assessed as reduction in cell viability incubated for 3 days at 37 °C by WST-1 colorimetric assay. Antiproliferative activity against human bladder carcinoma T24 cells assessed as reduction in cell viability incubated for 3 days at 37 °C by WST-1 colorimetric assay.	23742857
RBL-2H3	IC50	6.9 μM	Inhibition of antigen-induced beta-hexosaminidase release from RBL-2H3 cells incubated with DNP-BSA for 20 min and measured by absorbance at 405 nm. Inhibition of antigen-induced beta-hexosaminidase release from RBL-2H3 cells incubated with DNP-BSA for 20 min and measured by absorbance at 405 nm.	15256742
RBL-2H3	IC50	0.7 μM	Inhibition of antigen-induced TNF-alpha release from RBL-2H3 cells incubated with DNP-BSA for 4 hrs and measured by ELISA. Inhibition of antigen-induced TNF-alpha release from RBL-2H3 cells incubated with DNP-BSA for 4 hrs and measured by ELISA.	15256742
RBL-2H3	IC50	7.0 μM	Inhibition of antigen-induced IL-4 release from RBL-2H3 cells incubated with DNP-BSA for 4 hrs and measured by ELISA. Inhibition of antigen-induced IL-4 release from RBL-2H3 cells incubated with DNP-BSA for 4 hrs and measured by ELISA.	15256742

In Vitro

Rhinacanthin C binds to AMPKα and SIRT1 through hydrogen bonds and hydrophobic interactions, respectively, with binding energies of -5.63 and -3.93 kj/mol^[1].
Rhinacanthin C (0.25-2.0 μM; 3 days) dose-dependently inhibits RANKL-induced TRAP-positive multinucleated osteoclast formation and TRAP activity in mouse BMM cultures^[3].
Rhinacanthin C (1 μM; 3 days) reversibly inhibits the early-to-middle stages of RANKL-stimulated osteoclastogenesis in mouse BMMs^[3].
Rhinacanthin C (0.25-1.0 μM; 6 days) inhibits RANKL-stimulated bone resorption in mouse BMMs cultured on dentin slices^[3].
Rhinacanthin C (1 μM) inhibits RANKL-stimulated TRAF6-TAK1 complex formation in mouse BMMs^[3].
Rhinacanthin C (10 μM; 3 h) exhibits moderate permeability in Caco-2 cell monolayers^[5].
Rhinacanthin C (10-100 μM; 180 min) is a weak P-gp substrate and not a BCRP substrate in Caco-2 and MDCKII-BCRP cell monolayers^[5].
Rhinacanthin C (10 μM; 180 min) inhibits P-gp- and BCRP-mediated transport in Caco-2 and MDCKII-BCRP cell monolayers, with IC₅₀ values of 5.20 μM and 0.83 μM, respectively^[5].
Rhinacanthin C (10 μM; 30 min) inhibits OATP1B1- and OATP1B3-mediated uptake in HEK293-OATP1B1 and HEK293-OATP1B3 cells, with IC₅₀ values of 0.70 μM and 3.95 μM, respectively^[5].
Rhinacanthin C (0.1-50 μM; 10 min) inhibits CYP2C8, CYP2C9, and CYP2C19 in human liver microsomes, with IC₅₀ values of 4.45 μM, 1.57 μM, and 29.40 μM, respectively, but does not inhibit CYP1A2, CYP2A6, CYP2B6, CYP2D6, or CYP2E1^[5].
Rhinacanthin C (30 min)-mediated inhibition of CYP2C8, CYP2C9, and CYP2C19 in human liver microsomes is NADPH-independent, whereas CYP3A4/5 inhibition is NADPH-dependent when testosterone is used as the substrate^[5].
Rhinacanthin-C (1-100 μM; 1 day) upregulates P-gp expression by up to 1.74-fold without affecting its function, whereas prolonged exposure (7 days) has no effect on P-gp expression or function^[8].
Rhinacanthin C inhibits Saccharomyces cerevisiae α-glucosidase with an IC₅₀ of 22.6 μg/mL^[11].
Rhinacanthin C (12.5-50 μg/mL) exhibits non-competitive α-glucosidase inhibitory activity against Saccharomyces cerevisiae α-glucosidase^[11].
Rhinacanthin C (1/4IC₅₀, 1/2IC₅₀ and IC₅₀) combined with Acarbose (HY-B0089) at low concentrations exhibits synergistic inhibitory effects on Saccharomyces cerevisiae α-glucosidase^[11].
Rhinacanthin C interacts strongly with SOD (Libdock score 95.15) and GPx (Libdock score 105.24)^[2].
Rhinacanthin C (1 μM; 2 days) inhibits the induction of NFATc1, c-Fos, c-Src, and integrin β3 proteins in RANKL-stimulated mouse BMMs^[3].
Rhinacanthin C (1 μM) inhibits RANKL-mediated activation of the ERK, JNK, and NF-κB signaling axes in mouse BMMs, but does not inhibit p38^[3].
Rhinacanthin C (1 μM; 3 days) inhibits LPS-stimulated osteoclastogenesis in RANKL-pretreated mouse BMMs in a dose-dependent manner^[3].
Rhinacanthin-C (48 h) inhibited LPS-induced PGE₂ release in RAW264.7 cells with an IC₅₀ of 10.4 μM, but showed no activity against TNF-α release^[7].
Rhinacanthin C (0.25-0.5 μM; 1 h) protects primary rat hippocampal neurons against Aβ_25-35-induced cytotoxicity^[4].
Rhinacanthin C (0.5 μM; 1 h) promotes neurite outgrowth and restores neuronal integrity in Aβ-stimulated primary rat hippocampal neurons^[4].
RC (0.5 μM; 1 h) attenuates the toxic effects of Aβ-treated microglial conditioned medium on primary rat hippocampal neurons^[4].
Rhinacanthin C (0.5 μM) inhibits iNOS expression and NF-κB p65 nuclear translocation in LPS-stimulated rat glial cells^[4].
Rhinacanthin C (0.5 μM) inhibits the mRNA expression of inflammatory mediators Nos2, Il1b, Ccl2, Ccl5, and the microglial marker Iba1 in LPS-stimulated primary rat microglia^[4].
Rhinacanthin C (0.125-0.5 μM; 1 h) reduces IL-6 and TNF-α secretion by Aβ- and IFN-γ-activated BV-2 microglia^[4].
Rhinacanthin C (0.5 μM) inhibits CCL-2 secretion in BV-2 cells exposed to Aβ or IFN-γ^[4].
RC (0.5-1 μM; 4 h) abolishes NF-κB and ERK activation in Aβ- or IFN-γ-stimulated BV-2 microglia^[4].
Rhinacanthin-C (0.04-0.1 μM; 24-48 h) synergistically enhances the cytotoxicity of doxorubicin in MCF-7 cells, and the effect increases with prolonged treatment time (38.5-fold enhancement at 0.1 μM for 48 h)^[6].
Rhinacanthin-C (0.04-0.1 μM; up to 12 h) increases intracellular Doxorubicin (HY-15142A) accumulation in MCF-7 cells at 6 h^[6].
Rhinacanthin-C (0.1 μM; 2-12 h) interferes with MRP2 activity but not MRP1 activity in MCF-7 cells^[6].
Rhinacanthin-C (0.04-0.1 μM; 48 h) enhances the cytotoxicity of doxorubicin in doxorubicin-resistant MCF-7/DOX cells, with a 2.1-fold increase in sensitivity when 0.1 μM rhinacanthin-C is combined with 2 μM doxorubicin^[6].
Rhinacanthin-C (0.1 μM; 6 h) inhibits the activity of P-gp and MRP2 in MCF-7/DOX-resistant cells, increasing the intracellular accumulation of their substrates and doxorubicin^[6].
Rhinacanthin-C (0.156-400 μM; 1 day or 7 days) shows no cytotoxicity toward Caco-2 cells at concentrations up to 100 μM within 1 day and up to 0.625 μM within 7 days^[8].
Rhinacanthin-C (2.5-100 μM; 30 min) inhibits the function of P-gp and MRP2 in Caco-2 cells^[8].
Rhinacanthin C (various concentrations; 3 d) exhibited antiproliferative activity in HeLa and its MDR1-overexpressing subline Hvr100-6, with IC₅₀ values of 26.2 μM and 11.2 μM, respectively^[9].
Rhinacanthin C (various concentrations; 3 d) exhibited antiproliferative activity in PC-3 and T24 cells, with IC₅₀ values of 1.92 μM and 0.660 μM, respectively^[9].
Rhinacanthin C (3-100 μM; 10 min pre-incubation, 20 min antigen stimulation) effectively inhibits antigen-induced β-hexosaminidase release in RBL-2H3 cells, with an IC₅₀ of 6.9 μM^[10].
Rhinacanthin C (100 μM; 1 h) only weakly inhibited β-hexosaminidase enzyme activity in RBL-2H3 cell homogenates (100 μM^[10]).
Rhinacanthin C (0.3-30 μM; 4 h) effectively inhibits antigen-induced TNF-α release in RBL-2H3 cells, with an IC₅₀ of 0.7 μM^[10].
Rhinacanthin-C (compound 1) (1-100 μM; 48 h) effectively inhibits LPS-induced NO release in RAW264.7 cells, with an IC₅₀ of 1.8 μM^[7].
Rhinacanthin-C (10-30 μM; 20 h) inhibits LPS-induced iNOS and COX-2 gene expression in RAW264.7 cells in a concentration-dependent manner^[7].
Rhinacanthin C (1-100 μM; 4 h) inhibits antigen-induced IL-4 release in RBL-2H3 cells with an IC₅₀ of 7.0 μM^[10].
Rhinacanthin C (3-100 μM; 45 min) inhibits antigen-induced TNF-α and IL-4 mRNA expression in RBL-2H3 cells in a dose-dependent manner^[10].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.

Cell Differentiation Assay^[3]

View Protocol

Cell Line:

Mouse bone marrow macrophage (BMM) cultures
Concentration:

0.25, 0.5, 1.0, 2.0 μM
Incubation Time:

3 days
Result:

Produced dose-dependent inhibition of RANKL-induced TRAP-positive multinuclear osteoclast formation and TRAP activity from 0.25 to 2.0 μM.

Cell Differentiation Assay^[3]

View Protocol

Cell Line:

Mouse BMMs cultured on dentin slices
Concentration:

0.25, 0.5, 1.0 μM
Incubation Time:

6 days
Result:

Inhibited RANKL-stimulated bone resorption in a dose-dependent manner.

Western Blot Analysis^[3]

View Protocol

Cell Line:

Mouse BMMs
Concentration:

1 μM
Incubation Time:

2 days
Result:

Suppressed RANKL-stimulated induction of NFATc1 and c-Fos protein levels.
Suppressed RANKL-increased c-Src and integrin β3 expression.

Western Blot Analysis^[3]

View Protocol

Cell Line:

Mouse BMMs
Concentration:

1 μM
Incubation Time:

within 10 min
Result:

Suppressed RANKL-induced phosphorylation of IκB, NF-κB/p65, ERK, and JNK.
Did not suppress RANKL-induced phosphorylation of p38.

Cell Differentiation Assay^[3]

View Protocol

Cell Line:

RANKL-primed mouse BMMs
Concentration:

1 μM
Incubation Time:

3 days
Result:

Provided dose-dependent inhibition of LPS-stimulated osteoclastogenesis from BMMs.

Cell Viability Assay^[4]

View Protocol

Cell Line:

Primary rat hippocampal neurons
Concentration:

0.125, 0.25, 0.5, 1 μM
Incubation Time:

24 h
Result:

Revealed no significant toxicity with 0.125, 0.25, or 0.5 μM RC.
Chose concentrations at or below 0.5 μM for subsequent studies.

Cell Viability Assay^[4]

View Protocol

Cell Line:

Primary rat hippocampal neurons
Concentration:

0.25, 0.5 μM
Incubation Time:

1 h
Result:

Incubation with 25 μM Aβ25-35 for 24 h greatly decreased cell viability compared to control neurons.
Pretreatment of RC significantly reversed Aβ25-35-induced neuronal toxicity at concentrations of 0.25 μM and 0.5 μM.

Cell Differentiation Assay^[4]

View Protocol

Cell Line:

Primary rat hippocampal neurons
Concentration:

0.5 μM
Incubation Time:

1 h
Result:

Aβ significantly decreased neuronal integrity by an average of 50% after 24 h.
RC restored neuronal integrity in Aβ-treated hippocampal neurons to levels of untreated neurons.
Enhanced neurite outgrowth was observed in neurons incubated with 0.5 μM RC when compared to Aβ-treated neurons.

ELISA Assay^[4]

View Protocol

Cell Line:

Rat glial cultures (astrocytes and microglia)
Concentration:

0.5 μM
Incubation Time:

30 min
Result:

NO secretion was markedly increased upon treatment with 2 μg/mL LPS.
RC (0.5 μM) exposure for 30 min prior to LPS stimulation significantly inhibited NO production.
No effect on cell viability was observed after incubation with RC or/and LPS.

ELISA Assay^[4]

View Protocol

Cell Line:

BV-2 mouse microglial cell line
Concentration:

0.125, 0.25, 0.5 μM
Incubation Time:

1 h
Result:

IL-6 was elevated in microglia exposed to 20 μM Aβ or 100 pg/mL IFN-γ for 48 h, whereas pretreatment with RC (0.125, 0.25, 0.5 μM) significantly prevented IL-6 production.
RC treatment significantly reduced the secretion of TNF-α from BV-2 cells incubated with Aβ or IFN-γ without observed cytotoxicity.

ELISA Assay^[4]

View Protocol

Cell Line:

BV-2 mouse microglial cell line
Concentration:

0.5 μM
Incubation Time:

24 h
Result:

RC treatment showed a tendency to suppress CCL-5 production in BV-2 microglia exposed to Aβ but not to IFN-γ.
Pretreatment of BV-2 cells with 0.5 μM RC reduced the levels of CCL-2 induced by Aβ or IFN-γ.
This inhibition of cytokines was not due to cytotoxicity, as determined by LDH release assay.

Western Blot Analysis^[4]

View Protocol

Cell Line:

BV-2 mouse microglial cell line
Concentration:

0.5, 1 μM
Incubation Time:

4 h
Result:

RC at 0.5 and 1 μM reduced Aβ- or IFN-γ-activated NF-κB p65 phosphorylation.
RC reduced ERK activation in Aβ- or IFN-γ-activated BV-2 cells.

Immunofluorescence^[4]

View Protocol

Cell Line:

Primary rat hippocampal neurons
Concentration:

0.5 μM
Incubation Time:

1 h (RC pretreatment); 24 h (conditioned media)
Result:

Conditioned media from microglia exposed to 5 μM Aβ for 24 h reduced Tau immunoreactivity by 80% and decreased axon length by 75% compared to control.
Conditioned media from microglia pretreated with 0.5 μM RC restored neuronal integrity as demonstrated by increased Tau immunoreactivity and axon outgrowth.

Cell Viability Assay^[6]

View Protocol

Cell Line:

MCF-7
Concentration:

0.04, 0.1 μM
Incubation Time:

24, 48 h
Result:

Reduced the IC₅₀ of doxorubicin to 1.31 μM at 24 h and 0.08 μM at 48 h at 0.04 μM, with a CER of 1.04 at 24 h and 9.63 at 48 h and a CI of 0.97 at 24 h and 0.17 at 48 h.
Reduced the IC₅₀ of doxorubicin to 0.96 μM at 24 h and 0.02 μM at 48 h at 0.1 μM, with a CER of 1.42 at 24 h and 38.50 at 48 h and a CI of 0.71 at 24 h and 0.20 at 48 h.

Immunofluorescence^[6]

View Protocol

Cell Line:

MCF-7
Concentration:

0.04, 0.1 μM
Incubation Time:

up to 12 h
Result:

Increased doxorubicin accumulation significantly at 0.1 μM after 6 h treatment.
Did not significantly increase doxorubicin accumulation at 0.04 μM.

Cell Viability Assay^[6]

View Protocol

Cell Line:

MCF-7/DOX
Concentration:

0.04, 0.1 μM
Incubation Time:

48 h
Result:

Enhanced doxorubicin cytotoxicity, with the effect more pronounced at doxorubicin 2 μM than at 0.1 or 1 μM.
Increased sensitivity toward doxorubicin cytotoxicity by 2.1 fold at 0.1 μM combined with doxorubicin 2 μM.
Cell viability with rhinacanthin-C 0.1 μM was 86.57% (DOX 0.1 μM), 81.20% (DOX 1 μM), and 17.46% (DOX 2 μM).
Cell viability with rhinacanthin-C 0.04 μM was 90.70% (DOX 0.1 μM), 85.15% (DOX 1 μM), and 62.61% (DOX 2 μM).

Cell Cytotoxicity Assay^[8]

View Protocol

Cell Line:

RAW264.7
Concentration:

1, 3, 10, 30, 100 μM
Incubation Time:

48 h
Result:

Inhibited LPS-induced NO release with an IC₅₀ value of 1.8 μM.
Showed % inhibition of 0.0 at 0 μM, 32.1 at 1 μM, 60.5 at 3 μM, 92.1 at 10 μM, 97.5 at 30 μM, and 98.6 at 100 μM.

RT-PCR^[8]

View Protocol

Cell Line:

RAW264.7
Concentration:

10, 30 μM
Incubation Time:

20 h
Result:

Inhibited iNOS and COX-2 gene expressions in a concentration-dependent manner.

ELISA Assay^[11]

View Protocol

Cell Line:

RBL-2H3
Concentration:

0.3, 1, 3, 10, 30 μM
Incubation Time:

4 h
Result:

Inhibited antigen-induced TNF-α release with an IC₅₀ of 0.7 μM.
Showed % inhibition values of 0.0 at 0 μM, 21.1 at 0.3 μM, 60.3 at 1 μM, 93.3 at 3 μM, 93.5 at 10 μM, and 99.6 at 30 μM.

ELISA Assay^[11]

View Protocol

Cell Line:

RBL-2H3
Concentration:

3, 10, 30, 100 μM
Incubation Time:

4 h
Result:

Inhibited antigen-induced IL-4 release with an IC₅₀ of 7.0 μM.
Showed % inhibition values of 39.9 at 3 μM, 49.3 at 10 μM, 74.7 at 30 μM, and 100.4 at 100 μM.

RT-PCR^[11]

View Protocol

Cell Line:

RBL-2H3
Concentration:

3, 10, 30, 100 μM
Incubation Time:

45 min
Result:

Inhibited TNF-α and IL-4 mRNA expression in a dose-dependent manner.

In Vivo

Rhinacanthin C (5-20 mg/kg; oral; once daily; 12 weeks) ameliorates insulin resistance and lipid accumulation in HFD-induced NAFLD mice in a dose-dependent manner by activating AMPK/SIRT1 and inhibiting the SREBP-1c/FAS/ACC signaling pathway^[1].
Rhinacanthin C (5-20 mg/kg/day; oral; 28 days) lowered fasting blood glucose, HbA_1c, and lipid levels, increased serum insulin and pancreatic antioxidant enzyme levels, and ameliorated pancreatic histopathological changes in Streptozotocin (HY-13753)-Nicotinamide (HY-B0150)-induced diabetic rats^[2].
Rhinacanthin C (2 mg/kg; subcutaneous injection; daily; 5 days) prevents RANKL-induced calvarial bone destruction in vivo^[3].
Rhinacanthin C (2 mg/kg; subcutaneous injection; daily; 5 days) inhibits LPS-induced osteoclastogenesis and bone resorption^[3].
Rhinacanthin C (15 mg/kg; oral; once daily; 4 weeks) exerts protective effects against diabetic nephropathy in Streptozotocin-Nicotinamide-induced diabetic rats by alleviating renal oxidative stress, inflammation, lipid dysregulation, apoptosis, and histological damage^[12].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Animal Model:

C57BL/6JNifdc (male, wild-type, ~6 weeks old, 18-20 g)^[1]
Dosage:

5, 10, 20 mg/kg
Administration:

p.o.; once daily; 12 weeks
Result:

Inhibited HFD-induced body weight, liver weight, and liver/body weight ratio.
Reduced hepatic steatosis, inflammation, and ballooning, and decreased NAS scores.
Decreased AST and ALT.
Decreased hepatic TG and NEFA.
Decreased serum NEFA, TG, TC, and LDL-C while increasing serum HDL-C.
Reduced serum insulin, glucose, leptin, and resistin levels.
Increased hepatic ADIPOQ and ADIPOR2 expression.
Decreased HOMA-IR, OGTT, and ITT values.
Reduced hepatic and serum levels of MCP-1, TNF-α, and IL-6.
Decreased activities of SOD and GSH-Px, increased concentration of MDA, and upregulated mRNA expression of PPARα, ACOX1, and CPT-1α.
Upregulated p-AMPKα and SIRT1 and downregulated p-NF-κB p65 protein levels.
Downregulated protein expression levels of SREBP-1C, FAS, ACC, PPAR-γ, and SCD1.

Animal Model:

Sprague Dawley (adult male, 200-220 g)^[2]
Dosage:

5, 20 mg/kg/day
Administration:

p.o.; daily; 28 days
Result:

Decreased fasting blood glucose levels progressively from day 7 to day 28 in a dose-dependent manner.
Decreased serum HbA1c levels.
Increased serum insulin levels.
Decreased total cholesterol to 81.52 mmol/l (5 mg/kg) and 72.84 mmol/l (20 mg/kg).
Decreased triglycerides to 91.36 mmol/l (5 mg/kg) and 84.43 mmol/l (20 mg/kg).
Decreased LDL to 3.65 mmol/l (5 mg/kg) and 3.37 mmol/l (20 mg/kg).
Decreased VLDL to 18.27 mmol/l (5 mg/kg) and 16.88 mmol/l (20 mg/kg).
Increased HDL to 19.39 mmol/l (5 mg/kg) and 27.52 mmol/l (20 mg/kg).
Reduced LDL/HDL ratios to 0.73 (5 mg/kg) and 0.67 (20 mg/kg).
Reduced TC/HDL ratios to 0.14 (5 mg/kg) and 0.13 (20 mg/kg).
Decreased HOMA-IR index to 2.41 (5 mg/kg) and 2.27 (20 mg/kg) from 3.17.
Increased HOMA-β cell functioning index to 10.96 (5 mg/kg) and 14.38 (20 mg/kg) from 2.82.
Decreased pancreatic MDA levels to 9.83 µmoles/g wet weight (5 mg/kg) and 7.28 µmoles/g wet weight (20 mg/kg) from 14.65 µmoles/g wet weight.
Increased pancreatic SOD activity to 0.96 units/mg protein/min (5 mg/kg) and 1.32 units/mg protein/min (20 mg/kg) from 0.72 units/mg protein/min.
Increased pancreatic CAT activity to 0.37 (5 mg/kg) and 0.48 (20 mg/kg) from 0.29.
Increased pancreatic GPx activity to 1.24 (5 mg/kg) and 1.45 μmol GSH consumed/mg protein/min (20 mg/kg) from 0.89.
Increased final body weight to 196.18 g (5 mg/kg) and 201.72 g (20 mg/kg).
Decreased water intake to 37.32 mL/rat/day (5 mg/kg) and 31.75 mL/rat/day (20 mg/kg) from 47.64 mL/rat/day.
Decreased food intake to 27.54 g/rat/day (5 mg/kg) and 21.46 g/rat/day (20 mg/kg) from 34.39 g/rat/day.

Animal Model:

ddY mice (male, 8 weeks old)^[3]
Dosage:

2 mg/kg body weight
Administration:

s.c.; daily; 5 days
Result:

Reduced the RANKL-induced TRAP-positive area.
Significantly increased BV/TV and decreased trabecular separation compared to RANKL-injection alone.
Reduced the RANKL-induced increase of TBPf.

Animal Model:

C57BL/6 mice (male, 8 weeks old) and OPG-/- mice (male, 8 weeks old)^[3]
Dosage:

2 mg/kg body weight
Administration:

s.c.; daily; 5 days
Result:

Reduced LPS-induced osteoclast formation in both normal and OPG-/- mice.
Ameliorated LPS-induced calvarial bone resorption of normal and OPG knockout mice as shown by μCT analysis (BV/TV, Tb.Sp, and TBPf).

Animal Model:

Wistar (adult male, 200-250 g)^[12]
Dosage:

15 mg/kg
Administration:

p.o.; once daily; 4 weeks
Result:

Significantly decreased kidney index and reduced urinary albumin levels.
Reduced renal ROS and MDA levels and increased renal antioxidant enzyme activities of GSH, SOD, and CAT.
Attenuated increased renal levels of pro-inflammatory cytokines TNF-α, IL-1β, and IL-6.
Markedly decreased aberrant renal lipid profiles TG, FFA, and TC.
Significantly attenuated renal caspase-3 and cytochrome c concentrations.
Ameliorated thickening of the basement membrane of renal tubule and necrosis of renal tubules.

Chemical Information

CAS No. 159278-74-7
Molecular Weight 410.50
Formula C₂₅H₃₀O₅
SMILES

O=C1C2=CC=CC=C2C(C(O)=C1CC(C)(C)COC(/C(C)=C/CC/C(C)=C/C)=O)=O
Structure Classification
- Others
Initial Source
- Plants
- Acanthaceae
Shipping

Room temperature in continental US; may vary elsewhere.
Storage

Please store the product under the recommended conditions in the Certificate of Analysis.

Protocols

All Signal Pathway Related Molecular Biology Cell Biology Histomorphology Animals and Diseases

Kinase activity and phosphorylation assays
Kinase activity assays measure the ability of kinases to transfer phosphate groups from ATP to specific substrates, while phosphorylation assays detect the presence and levels of phosphorylated proteins. Common methods include radiolabeled ATP incorporation (e. g. ,), ADP release detection via bioluminescence (e. g. ,[3]), enzyme-linked immunosorbent assays (ELISA) for phospho-specific epitopes (e. g. ,[6]), and microtiter-based formats for high-throughput screening (e. g. ,[8]). The ADP-Glo assay quantifies kinase activity by measuring ADP produced during phosphorylation using a luciferase-based system. Radiometric assays involve autoradiography or scintillation counting after incorporation of ³²P-labeled ATP into substrate proteins. ELISA-based approaches rely on phospho-specific antibodies to detect activated kinases in cell lysates or purified samples.
Western Blot
Western blotting (WB) is a commonly used experimental method in molecular biology, biochemistry, and immunogenetics for identifying and quantifying target proteins. It combines gel electrophoresis with immunoassay, enabling researchers to analyze protein expression, post-translational modifications, and molecular weight.
Cell Cytotoxicity Assay
Cytotoxicity assays are usually based on the assessment of cell membrane damage, which can also be indirectly detected by measuring cell viability. Detection methods include MTT assay, CKK-8 assay, LDH assay and ATP assay, etc.
Research Protocol for Endocrine Diseases
Endocrine diseases often arise from disrupted hormone production, hormone signaling, or target-tissue responsiveness; for diabetes-focused endocrine disease models, insulin signaling regulates glucose uptake, hepatic glucose output, lipid metabolism, and β-cell compensation. Type 2 diabetes develops through interacting defects in insulin resistance, β-cell dysfunction, adipose inflammation, hepatic glucose overproduction, altered incretin signaling, and ectopic lipid metabolism. A major unresolved question is whether endocrine dysfunction is driven primarily by target-tissue insulin resistance, intrinsic β-cell failure, immune/inflammatory stress, or combined multi-organ failure that differs by disease stage.
Research Protocol for Inflammation-related Diseases
The NLRP3 inflammasome is a cytosolic innate immune signaling platform that integrates priming signals and danger-signal activation to promote caspase-1 activation, maturation of IL-1β and IL-18, and gasdermin D-mediated pyroptotic cell death. The core experimental logic is to determine whether inflammatory disease phenotypes are driven by increased NLRP3 expression, ASC-containing inflammasome assembly, caspase-1 cleavage, GSDMD cleavage, and extracellular release of IL-1β/IL-18 rather than by nonspecific cell injury alone. The pathway is strongly linked to inflammation-related disease phenotypes because monosodium urate crystals activate NALP3/NLRP3 inflammasome signaling in gout-like crystal inflammation, cholesterol crystals activate NLRP3 inflammasomes in atherogenesis models, and DSS-induced intestinal inflammation has been reported to involve NLRP3 inflammasome activity. However, experimental colitis studies also show context-dependent protective effects of NLRP3 inflammasome co
Protocol for Kinase activity and phosphorylation assays
Kinase activity assays measure transfer of phosphate from ATP to a protein or peptide substrate, generating phosphorylated substrate, ADP, or incorporated radiolabeled phosphate as the readout; phosphorylation assays measure site-specific phosphorylation in cells or tissues as a proxy for kinase-pathway activation, inhibition, or substrate regulation. Phosphorylation can be detected by phospho-specific Western blot, immunoprecipitation kinase assay, phospho-immunofluorescence, phospho-flow cytometry, luminescent ADP detection, radiolabeled ATP incorporation, or reporter-based pathway assays, and these readouts can be applied to cancer cells, primary neurons, mouse tumors, organoids, inflammatory macrophages, ferroptosis studies, and mitophagy studies when the kinase target is biologically relevant.
Research Protocol for Metabolic Diseases
AMP-activated protein kinase, AMPK, is a conserved cellular energy sensor that responds to reduced cellular energy status and coordinates metabolism by increasing ATP-generating catabolic pathways while suppressing ATP-consuming anabolic processes. In metabolic disease research, the AMPK pathway is experimentally relevant because it regulates hepatic lipid synthesis, fatty acid oxidation, glucose production, skeletal-muscle glucose disposal, mTORC1-linked biosynthesis, autophagy, mitochondrial homeostasis, and whole-body energy balance. The central pathway logic is that energy stress, metformin, exercise-like stimulation, or direct AMPK activators increase AMPKα Thr172 phosphorylation and downstream substrate phosphorylation, including ACC and RAPTOR. Phosphorylation of ACC suppresses lipogenesis and supports fatty acid oxidation, whereas phosphorylation of RAPTOR suppresses mTORC1 signaling and links cellular energy status to growth and protein synthesis control. The pathway is linked
Liver Histomorphometry
Liver histomorphometry is a quantitative histological approach used to measure structural alterations in hepatic tissue, including parenchymal loss, steatosis, fibrosis, and vascular remodeling, by combining stained tissue section analysis with stereological or computerized image-based measurements. Classical morphometric frameworks quantify volume fractions of liver compartments and fibrotic regions using systematic sampling and image analysis, enabling objective comparison of pathological changes across experimental groups. These approaches are widely applied in liver cirrhosis and fibrosis studies to reduce subjectivity in histological scoring and improve reproducibility of tissue evaluation. Recent methodological advances integrate automated image analysis and radiomics-based extraction of histological features from standard liver stains (e. g. , H&E and fibrotic stains), enabling quantitative correlation between morphometric features and fibrosis stages in non-alcoholic fatty live
Alzheimer’s Disease Modeling
Alzheimer’s Disease (AD) is a neurodegenerative disorder characterized by a progressive decline in cognitive functions and loss of specific types of neurons and synapses. Alzheimer's symptoms can be simulated in mice by injecting drugs (such as Aβ) or genetically modified.

Purity & Documentation

Handling Instructions (2659 KB)

References

[1]. Gong Z, et al. Rhinacanthin C Ameliorates Insulin Resistance and Lipid Accumulation in NAFLD Mice via the AMPK/SIRT1 and SREBP-1c/FAS/ACC Signaling Pathways. Evid Based Complement Alternat Med. 2023 Jan 10;2023:6603522.

[2]. Adam SH, et al. Rhinacanthin C ameliorates hyperglycaemia, hyperlipidemia and pancreatic destruction in streptozotocin-nicotinamide induced adult male diabetic rats. European journal of pharmacology. 2016 Jan 15;771:173-90.

[3]. Tomomura M, et al. Rhinacanthin C Inhibits Osteoclast Differentiation and Bone Resorption: Roles of TRAF6/TAK1/MAPKs/NF-κB/NFATc1 Signaling. PLoS One. 2015 Jun 17;10(6):e0130174.

[4]. Chuang KA, et al. Rhinacanthin C Alleviates Amyloid- Fibrils' Toxicity on Neurons and Attenuates Neuroinflammation Triggered by LPS, Amyloid-, and Interferon- in Glial Cells. Oxidative medicine and cellular longevity. 2017;2017:5414297.

[5]. Dunkoksung W, et al. Rhinacanthin-C Mediated Herb-Drug Interactions with Drug Transporters and Phase I Drug-Metabolizing Enzymes. Drug metabolism and disposition: the biological fate of chemicals. 2019 Oct;47(10):1040-1049.

[6]. Chaisit T, et al. Rhinacanthin-C enhances doxorubicin cytotoxicity via inhibiting the functions of P-glycoprotein and MRP2 in breast cancer cells. European journal of pharmacology. 2017 Jan 15;795:50-57.

[7]. Tewtrakul S, et al. Effects of rhinacanthins from Rhinacanthus nasutus on nitric oxide, prostaglandin E2 and tumor necrosis factor-alpha releases using RAW264.7 macrophage cells. Phytomedicine : international journal of phytotherapy and phytopharmacology. 2009 Jun;16(6-7):581-5.

[8]. Wongwanakul R, et al. Effects of rhinacanthin-C on function and expression of drug efflux transporters in Caco-2 cells. Fitoterapia. 2013 Sep;89:80-5.

[9]. Gotoh A, et al. Antiproliferative activity of Rhinacanthus nasutus (L.) Kurz extracts and the active moiety, Rhinacanthin C. Biological & pharmaceutical bulletin. 2004 Jul;27(7):1070-4.

[10]. Tewtrakul S, et al. Anti-allergic principles of Rhinacanthus nasutus leaves. Phytomedicine : international journal of phytotherapy and phytopharmacology. 2009 Oct;16(10):929-34.

[11]. Muhammad Ajmal Shah, et al.
α-Glucosidase inhibitory effect of rhinacanthins-rich extract from Rhinacanthus nasutus leaf and synergistic effect in combination with acarbose, Journal of Functional Foods, Volume 36, 2017, Pages 325-331, ISSN 1756-4646.

[12]. Zhao LL, et al. Rhinacanthins-rich extract and rhinacanthin C ameliorate oxidative stress and inflammation in streptozotocin-nicotinamide-induced diabetic nephropathy. Journal of food biochemistry. 2019 Apr;43(4):e12812.

Calculators

Molarity Calculator

Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)

Mass Mass

Concentration Concentration

Volume Volume

Molecular Weight Molecular Weight

Dilution Calculator

Concentration _(start) × Volume _(start) = Concentration _(final) × Volume _(final)

Concentration _(start) Concentration _(start)

Volume _(start) Volume _(start)

Concentration _(final) Concentration _(final)

Volume _(final) Volume _(final)

Help & FAQs

How should lyophilized recombinant proteins be reconstituted and stored?

1. Before opening the cap, centrifuge the vial at 13000 rpm for 20-30 seconds. This step will ensure that any lyophilized powder that may have adhered to the cap or walls is collected at the bottom of the vial, minimizing the risk of product loss.

Product Name:
Cat. No.:
Quantity:
MCE Japan Authorized Agent:

Product Name:
CAS No.:
Species:
Purity:
Quantity:

Rhinacanthin C

All AMPK Isoforms

All Sirtuin Isoforms