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recombinant human md2 rhmd2 protein (R&D Systems)

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R&D Systems recombinant human md2 rhmd2 protein
Interaction of GA monomers with the <t>MD2/TLR4</t> complex. (A–H) Surface plasmon resonance (SPR) analysis showing direct binding of Ganoderic acid A, B, C2, C6, G, H, K, and Ganoderenic acid B to MD2. (I) Binding of GA‐A to MD2 as assessed by protein microarray analysis. (J) Identification of MD2/TLR4 complexes via immunoprecipitation.

Interaction of GA monomers with the <t>MD2/TLR4</t> complex. (A–H) Surface plasmon resonance (SPR) analysis showing direct binding of Ganoderic acid A, B, C2, C6, G, H, K, and Ganoderenic acid B to MD2. (I) Binding of GA‐A to MD2 as assessed by protein microarray analysis. (J) Identification of MD2/TLR4 complexes via immunoprecipitation.

Recombinant Human Md2 Rhmd2 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+md2+rhmd2+protein/pmc12970185-152-10-15?v=R%26D+Systems
Average 94 stars, based on 25 article reviews

recombinant human md2 rhmd2 protein - by Bioz Stars, 2026-07

94/100 stars

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1) Product Images from "Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy"

Article Title: Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy

Journal: Exploration

doi: 10.1002/EXP.20240147

Interaction of GA monomers with the MD2/TLR4 complex. (A–H) Surface plasmon resonance (SPR) analysis showing direct binding of Ganoderic acid A, B, C2, C6, G, H, K, and Ganoderenic acid B to MD2. (I) Binding of GA‐A to MD2 as assessed by protein microarray analysis. (J) Identification of MD2/TLR4 complexes via immunoprecipitation.

Figure Legend Snippet: Interaction of GA monomers with the MD2/TLR4 complex. (A–H) Surface plasmon resonance (SPR) analysis showing direct binding of Ganoderic acid A, B, C2, C6, G, H, K, and Ganoderenic acid B to MD2. (I) Binding of GA‐A to MD2 as assessed by protein microarray analysis. (J) Identification of MD2/TLR4 complexes via immunoprecipitation.

Techniques Used: SPR Assay, Binding Assay, Microarray, Immunoprecipitation

Molecular docking of GA‐K with MD2 and its effect on cerebral ischemic injury in the mouse tMCAO model. (A) Molecular docking of GA‐K (yellow) with the MD2 protein (green), analyzed using the Trips molecular modeling software. (B) Representative coronal brain sections stained with TTC, showing typical infarct areas in white. Scale bar = 5 mm. (C) Quantification of infarct volume. (D) Neurological deficit scores quantification. The data are presented as the mean ± SEM ( n = 8). Statistical significance: ** p < 0.01 compared to the tMCAO group.

Figure Legend Snippet: Molecular docking of GA‐K with MD2 and its effect on cerebral ischemic injury in the mouse tMCAO model. (A) Molecular docking of GA‐K (yellow) with the MD2 protein (green), analyzed using the Trips molecular modeling software. (B) Representative coronal brain sections stained with TTC, showing typical infarct areas in white. Scale bar = 5 mm. (C) Quantification of infarct volume. (D) Neurological deficit scores quantification. The data are presented as the mean ± SEM ( n = 8). Statistical significance: ** p < 0.01 compared to the tMCAO group.

Techniques Used: Software, Staining

GAs suppress MD2/TLR4 complex formation and inhibit MAPK and NF‐κB signaling pathways in a mouse model of tMCAO. GA (administered at doses of 0 or 20 mg kg −1 , i.p.) was given immediately after reperfusion. At 24 h post‐reperfusion, total and nuclear proteins were isolated from the cortical penumbra for analysis by Western blotting. (A) Immunoprecipitation analysis of the MD2/TLR4 complex in the ischemic hemisphere. (B) Quantification of MD2 expression levels. (C) Representative Western blot images showing proteins involved in the MAPK signaling pathway. (D) Quantitative analysis of phosphorylation levels. (E) Representative Western blot images of nuclear NF‐κB and AP‐1. (F) Quantification of protein expression. The data are presented as the mean ± SEM ( n = 4). Statistical significance is indicated as follows: ### p < 0.001 compared to the sham group, * p < 0.05, ** p < 0.01 compared to the vehicle‐treated tMCAO group.

Figure Legend Snippet: GAs suppress MD2/TLR4 complex formation and inhibit MAPK and NF‐κB signaling pathways in a mouse model of tMCAO. GA (administered at doses of 0 or 20 mg kg −1 , i.p.) was given immediately after reperfusion. At 24 h post‐reperfusion, total and nuclear proteins were isolated from the cortical penumbra for analysis by Western blotting. (A) Immunoprecipitation analysis of the MD2/TLR4 complex in the ischemic hemisphere. (B) Quantification of MD2 expression levels. (C) Representative Western blot images showing proteins involved in the MAPK signaling pathway. (D) Quantitative analysis of phosphorylation levels. (E) Representative Western blot images of nuclear NF‐κB and AP‐1. (F) Quantification of protein expression. The data are presented as the mean ± SEM ( n = 4). Statistical significance is indicated as follows: ### p < 0.001 compared to the sham group, * p < 0.05, ** p < 0.01 compared to the vehicle‐treated tMCAO group.

Techniques Used: Protein-Protein interactions, Isolation, Western Blot, Immunoprecipitation, Expressing, Phospho-proteomics

MD2 knockout reduces microglia activation and improves acute cerebral ischemic injury in the tMCAO mouse model. (A) Representative micrographs (magnification ×100) showing immunofluorescent staining of MD2 (red) in the peri‐infarct area of the cortex and the dentate gyrus of the hippocampus, 24 h after reperfusion. Scale bars: 50 µm. WT and MD2‐KO mice underwent 1 h of tMCAO, followed by 24 h of reperfusion. GA (0 or 20 mg kg −1 , i.p.) was administered immediately post‐reperfusion. (B) Representative micrographs depicting immunofluorescence for Iba‐1 (green). Primary microglial cells were isolated from WT and MD2‐KO mice, pretreated with GA (50 µg mL −1 ) or vehicle for 1 h, then stimulated with LPS (10 ng mL −1 ) for 12 h. (C) Representative Western blots illustrating levels of p‐JNK, p‐ERK, p‐P38, and p‐NF‐κB. (D) Representative Western blots for inflammatory mediators iNOS, COX‐2, and TNF‐α ( n = 4). (E) Representative coronal brain sections stained with TTC. Infarct areas appear white. Bar = 5 mm. (F) Infarction volume assessment. (G) Neurological deficit score quantification. The data are presented as the mean ± SEM ( n = 8). Statistical significance is indicated as follows: * * P < 0.01, ** * P < 0.001 compared to the WT tMCAO group.

Figure Legend Snippet: MD2 knockout reduces microglia activation and improves acute cerebral ischemic injury in the tMCAO mouse model. (A) Representative micrographs (magnification ×100) showing immunofluorescent staining of MD2 (red) in the peri‐infarct area of the cortex and the dentate gyrus of the hippocampus, 24 h after reperfusion. Scale bars: 50 µm. WT and MD2‐KO mice underwent 1 h of tMCAO, followed by 24 h of reperfusion. GA (0 or 20 mg kg −1 , i.p.) was administered immediately post‐reperfusion. (B) Representative micrographs depicting immunofluorescence for Iba‐1 (green). Primary microglial cells were isolated from WT and MD2‐KO mice, pretreated with GA (50 µg mL −1 ) or vehicle for 1 h, then stimulated with LPS (10 ng mL −1 ) for 12 h. (C) Representative Western blots illustrating levels of p‐JNK, p‐ERK, p‐P38, and p‐NF‐κB. (D) Representative Western blots for inflammatory mediators iNOS, COX‐2, and TNF‐α ( n = 4). (E) Representative coronal brain sections stained with TTC. Infarct areas appear white. Bar = 5 mm. (F) Infarction volume assessment. (G) Neurological deficit score quantification. The data are presented as the mean ± SEM ( n = 8). Statistical significance is indicated as follows: * * P < 0.01, ** * P < 0.001 compared to the WT tMCAO group.

Techniques Used: Knock-Out, Activation Assay, Staining, Immunofluorescence, Isolation, Western Blot

Proposed mechanism of GA in alleviating cerebral ischemic injury. GA monomers interact directly with MD2, preventing the dimerization of MD2 and TLR4, as well as the subsequent activation of downstream MAPK and NF‐κB signaling pathways. This process lowers inflammatory mediator production and reduces microglial overactivation.

Figure Legend Snippet: Proposed mechanism of GA in alleviating cerebral ischemic injury. GA monomers interact directly with MD2, preventing the dimerization of MD2 and TLR4, as well as the subsequent activation of downstream MAPK and NF‐κB signaling pathways. This process lowers inflammatory mediator production and reduces microglial overactivation.

Techniques Used: Activation Assay, Protein-Protein interactions

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Journal: Exploration

Article Title: Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy

doi: 10.1002/EXP.20240147

Figure Lengend Snippet: Interaction of GA monomers with the MD2/TLR4 complex. (A–H) Surface plasmon resonance (SPR) analysis showing direct binding of Ganoderic acid A, B, C2, C6, G, H, K, and Ganoderenic acid B to MD2. (I) Binding of GA‐A to MD2 as assessed by protein microarray analysis. (J) Identification of MD2/TLR4 complexes via immunoprecipitation.

Article Snippet: To investigate the molecular interaction between GA monomers and MD2, recombinant human MD2 (rhMD2) protein (R&D Systems) was employed.

Techniques: SPR Assay, Binding Assay, Microarray, Immunoprecipitation

Journal: Exploration

Article Title: Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy

doi: 10.1002/EXP.20240147

Figure Lengend Snippet: Molecular docking of GA‐K with MD2 and its effect on cerebral ischemic injury in the mouse tMCAO model. (A) Molecular docking of GA‐K (yellow) with the MD2 protein (green), analyzed using the Trips molecular modeling software. (B) Representative coronal brain sections stained with TTC, showing typical infarct areas in white. Scale bar = 5 mm. (C) Quantification of infarct volume. (D) Neurological deficit scores quantification. The data are presented as the mean ± SEM ( n = 8). Statistical significance: ** p < 0.01 compared to the tMCAO group.

Article Snippet: To investigate the molecular interaction between GA monomers and MD2, recombinant human MD2 (rhMD2) protein (R&D Systems) was employed.

Techniques: Software, Staining

Journal: Exploration

Article Title: Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy

doi: 10.1002/EXP.20240147

Figure Lengend Snippet: GAs suppress MD2/TLR4 complex formation and inhibit MAPK and NF‐κB signaling pathways in a mouse model of tMCAO. GA (administered at doses of 0 or 20 mg kg −1 , i.p.) was given immediately after reperfusion. At 24 h post‐reperfusion, total and nuclear proteins were isolated from the cortical penumbra for analysis by Western blotting. (A) Immunoprecipitation analysis of the MD2/TLR4 complex in the ischemic hemisphere. (B) Quantification of MD2 expression levels. (C) Representative Western blot images showing proteins involved in the MAPK signaling pathway. (D) Quantitative analysis of phosphorylation levels. (E) Representative Western blot images of nuclear NF‐κB and AP‐1. (F) Quantification of protein expression. The data are presented as the mean ± SEM ( n = 4). Statistical significance is indicated as follows: ### p < 0.001 compared to the sham group, * p < 0.05, ** p < 0.01 compared to the vehicle‐treated tMCAO group.

Article Snippet: To investigate the molecular interaction between GA monomers and MD2, recombinant human MD2 (rhMD2) protein (R&D Systems) was employed.

Techniques: Protein-Protein interactions, Isolation, Western Blot, Immunoprecipitation, Expressing, Phospho-proteomics

Journal: Exploration

Article Title: Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy

doi: 10.1002/EXP.20240147

Figure Lengend Snippet: MD2 knockout reduces microglia activation and improves acute cerebral ischemic injury in the tMCAO mouse model. (A) Representative micrographs (magnification ×100) showing immunofluorescent staining of MD2 (red) in the peri‐infarct area of the cortex and the dentate gyrus of the hippocampus, 24 h after reperfusion. Scale bars: 50 µm. WT and MD2‐KO mice underwent 1 h of tMCAO, followed by 24 h of reperfusion. GA (0 or 20 mg kg −1 , i.p.) was administered immediately post‐reperfusion. (B) Representative micrographs depicting immunofluorescence for Iba‐1 (green). Primary microglial cells were isolated from WT and MD2‐KO mice, pretreated with GA (50 µg mL −1 ) or vehicle for 1 h, then stimulated with LPS (10 ng mL −1 ) for 12 h. (C) Representative Western blots illustrating levels of p‐JNK, p‐ERK, p‐P38, and p‐NF‐κB. (D) Representative Western blots for inflammatory mediators iNOS, COX‐2, and TNF‐α ( n = 4). (E) Representative coronal brain sections stained with TTC. Infarct areas appear white. Bar = 5 mm. (F) Infarction volume assessment. (G) Neurological deficit score quantification. The data are presented as the mean ± SEM ( n = 8). Statistical significance is indicated as follows: * * P < 0.01, ** * P < 0.001 compared to the WT tMCAO group.

Article Snippet: To investigate the molecular interaction between GA monomers and MD2, recombinant human MD2 (rhMD2) protein (R&D Systems) was employed.

Techniques: Knock-Out, Activation Assay, Staining, Immunofluorescence, Isolation, Western Blot

Journal: Exploration

Article Title: Ganoderic Acids Alleviate Neuroinflammation by Targeting Myeloid Differentiation Factor 2 for Ischemic Stroke Therapy

doi: 10.1002/EXP.20240147

Figure Lengend Snippet: Proposed mechanism of GA in alleviating cerebral ischemic injury. GA monomers interact directly with MD2, preventing the dimerization of MD2 and TLR4, as well as the subsequent activation of downstream MAPK and NF‐κB signaling pathways. This process lowers inflammatory mediator production and reduces microglial overactivation.

Article Snippet: To investigate the molecular interaction between GA monomers and MD2, recombinant human MD2 (rhMD2) protein (R&D Systems) was employed.

Techniques: Activation Assay, Protein-Protein interactions

Exercise blocks MD2-TLR4 pathway activation in mouse livers. ( A ) MD2-TLR4 complex formation levels in mouse liver tissues detected by co-immunoprecipitation. ( B ) Protein levels of MAPK pathway and NF-κB pathway components, including p-ERK, p-JNK, p-p38, p-p65, and IκB-α. The corresponding unphosphorylated proteins and tubulin were used as the loading controls. ( C ) Relative mRNA levels of several pro-inflammatory markers Il6, Il1b, Tnf, Ccl2, Icam1, and Vcam1 in mouse liver tissues. The data are presented as the mean ± SEM, n = 6 per group. # p < 0.05 vs. NCD group; * p < 0.05 vs. HFD group.

Journal: Cells

Article Title: Exercise-Induced Irisin Decreases Inflammation and Improves NAFLD by Competitive Binding with MD2

doi: 10.3390/cells10123306

Figure Lengend Snippet: Exercise blocks MD2-TLR4 pathway activation in mouse livers. ( A ) MD2-TLR4 complex formation levels in mouse liver tissues detected by co-immunoprecipitation. ( B ) Protein levels of MAPK pathway and NF-κB pathway components, including p-ERK, p-JNK, p-p38, p-p65, and IκB-α. The corresponding unphosphorylated proteins and tubulin were used as the loading controls. ( C ) Relative mRNA levels of several pro-inflammatory markers Il6, Il1b, Tnf, Ccl2, Icam1, and Vcam1 in mouse liver tissues. The data are presented as the mean ± SEM, n = 6 per group. # p < 0.05 vs. NCD group; * p < 0.05 vs. HFD group.

Article Snippet: Recombinant irisin was purchased from Phoenix Pharmaceuticals (Burlingame, CA, USA) and recombinant human MD2 (rhMD2) was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Activation Assay, Immunoprecipitation

Irisin blocks NF-κB and MAPK pathways, and reduces inflammatory factors in AML12 cells. ( A , B ) AML12 cells were pretreated with recombinant irisin (50 or 100 ng/mL) for 30 min followed by exposure to 200 μM PA for 2 h. ( A ) MD2-TLR4 complex formation levels in AML12 cells detected by immunoprecipitation. ( B ) Protein levels of MAPK pathway and NF-κB pathway components, including p-ERK, p-JNK, p-p38, p-p65, and IκB-α. The corresponding unphosphorylated proteins and tubulin were used as loading controls. ( C ) AML12 cells were pretreated with recombinant irisin (50 or 100 ng/mL) for 30 min followed by exposure to 200 μM PA for 12 h. Relative mRNA levels of Il6, Il1b, Tnf, Ccl2, Icam1, and Vcam1 were detected. The data are presented as the mean ± SEM. # p < 0.05 vs. CON group; * p < 0.05 vs. PA group.

Journal: Cells

Article Title: Exercise-Induced Irisin Decreases Inflammation and Improves NAFLD by Competitive Binding with MD2

doi: 10.3390/cells10123306

Figure Lengend Snippet: Irisin blocks NF-κB and MAPK pathways, and reduces inflammatory factors in AML12 cells. ( A , B ) AML12 cells were pretreated with recombinant irisin (50 or 100 ng/mL) for 30 min followed by exposure to 200 μM PA for 2 h. ( A ) MD2-TLR4 complex formation levels in AML12 cells detected by immunoprecipitation. ( B ) Protein levels of MAPK pathway and NF-κB pathway components, including p-ERK, p-JNK, p-p38, p-p65, and IκB-α. The corresponding unphosphorylated proteins and tubulin were used as loading controls. ( C ) AML12 cells were pretreated with recombinant irisin (50 or 100 ng/mL) for 30 min followed by exposure to 200 μM PA for 12 h. Relative mRNA levels of Il6, Il1b, Tnf, Ccl2, Icam1, and Vcam1 were detected. The data are presented as the mean ± SEM. # p < 0.05 vs. CON group; * p < 0.05 vs. PA group.

Article Snippet: Recombinant irisin was purchased from Phoenix Pharmaceuticals (Burlingame, CA, USA) and recombinant human MD2 (rhMD2) was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Recombinant, Immunoprecipitation

Irisin competitively binds to MD2 but not TLR4. ( A , B ) Immunoprecipitation analysis of the binding ability of recombinant irisin to MD2 ( A ) or TLR4 ( B ) in liver lysates. ( C ) ELISA analysis in the binding ability of recombinant irisin to MD2 or TLR4 in liver lysates. ( D ) Immunoprecipitation analysis in the binding ability of recombinant irisin to rhMD2. ( E ) ELISA analysis of the binding ability of recombinant irisin to rhMD2. ( F ) Surface plasmon resonance analysis between irisin with rhMD2. ( G ) ELISA analysis of the effect of recombinant irisin (0.1, 0.2, and 0.5 μg/mL) on the basal binding level of MD2-TLR4. ( H , I ) ELISA analysis of the competitive MD2 binding ability of recombinant irisin (0.1, 0.2, and 0.5 μg/mL) to PA or LPS. ( J ) Molecular docking of the dimeric irisin-MD2 complex. ( K ) ELISA analysis of irisin-MD2 binding levels in mouse liver tissue ( n = 6 per group). The data are presented as the mean ± SEM. # p < 0.05 vs. CON or NCD group; * p < 0.05 vs. rhMD2 or HFD group.

Journal: Cells

Article Title: Exercise-Induced Irisin Decreases Inflammation and Improves NAFLD by Competitive Binding with MD2

doi: 10.3390/cells10123306

Figure Lengend Snippet: Irisin competitively binds to MD2 but not TLR4. ( A , B ) Immunoprecipitation analysis of the binding ability of recombinant irisin to MD2 ( A ) or TLR4 ( B ) in liver lysates. ( C ) ELISA analysis in the binding ability of recombinant irisin to MD2 or TLR4 in liver lysates. ( D ) Immunoprecipitation analysis in the binding ability of recombinant irisin to rhMD2. ( E ) ELISA analysis of the binding ability of recombinant irisin to rhMD2. ( F ) Surface plasmon resonance analysis between irisin with rhMD2. ( G ) ELISA analysis of the effect of recombinant irisin (0.1, 0.2, and 0.5 μg/mL) on the basal binding level of MD2-TLR4. ( H , I ) ELISA analysis of the competitive MD2 binding ability of recombinant irisin (0.1, 0.2, and 0.5 μg/mL) to PA or LPS. ( J ) Molecular docking of the dimeric irisin-MD2 complex. ( K ) ELISA analysis of irisin-MD2 binding levels in mouse liver tissue ( n = 6 per group). The data are presented as the mean ± SEM. # p < 0.05 vs. CON or NCD group; * p < 0.05 vs. rhMD2 or HFD group.

Article Snippet: Recombinant irisin was purchased from Phoenix Pharmaceuticals (Burlingame, CA, USA) and recombinant human MD2 (rhMD2) was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Immunoprecipitation, Binding Assay, Recombinant, Enzyme-linked Immunosorbent Assay, SPR Assay

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