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recombinant human md2 rhmd2 protein  (R&D Systems)


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    Structured Review

    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.
    Recombinant Human Md2 Rhmd2 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+md+2/Recombinant+Human+MD-2+Protein/pmc12970185-152-10-15
    Average 94 stars, based on 28 article reviews
    recombinant human md2 rhmd2 protein - by Bioz Stars, 2026-09
    94/100 stars

    Images

    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

    Related Articles

    Binding Assay:

    Article Title: Simultaneous Control of Infection and Inflammation by Keratin-Derived Antibacterial Peptides (KAMPs) Targeting TLRs and Co-Receptors
    Article Snippet: One quarter of the bead suspension was mixed with 50 μl of PBS containing 25 μg of recombinant human TLR4/MD-2 complex or TLR2 (R&D) for 3 hours at 25 ° C. Following conjugation, beads were washed with PBS and stored in 100 μl of QBS buffer (PBS containing 1% BSA and 0.02% sodium azide). .. To assess KAMPs binding to TLR4/MD-2, TLR4/MD-2 complex-conjugated beads (5,000 in FACS buffer) were preincubated with KAMP-10 (48 μg/ml), KAMP-18C (96 μg/ml) or SC-10 (48 μg/ml) in the presence or absence of recombinant human MD-2 (R&D) (1 μg/ml) for 1 h on ice. .. Beads were then washed twice with PBS before incubation with FITC-E. coli O55:B5 LPS (1 μg/ml) (Sigma-Aldrich) for 1 h on ice.

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    Article Title: The matricellular protein SPARC induces inflammatory interferon-response in macrophages during aging.
    Article Snippet: .. Nunc Maxisorp 96-well plates (Thermo Fischer Scientific) were coated with 100 mL solution containing 0.25, 2.5, and 25 mg/mL of each hTLR4 (R&D), hTLR2 (R&D), human MD-2 (R&D), mTLR4 (CUSABIO), and BSA (Bio-Rad) in PBS and incubated overnight at 4 C. After washing with washing buffer (PBST, Tween 20 0.05%) three times, unspecific binding was blocked with 10% BSA in PBST (0.05% Tween 20) for 1 h at room temperature. .. Following three times of washing, 20 mg/mL SPARC recombinant proteins (Peprotech) were added in 2% BSA/PBST, incubated for 2 h at room temperature, and washed three times.

    FACS:

    Article Title: Simultaneous Control of Infection and Inflammation by Keratin-Derived Antibacterial Peptides (KAMPs) Targeting TLRs and Co-Receptors
    Article Snippet: One quarter of the bead suspension was mixed with 50 μl of PBS containing 25 μg of recombinant human TLR4/MD-2 complex or TLR2 (R&D) for 3 hours at 25 ° C. Following conjugation, beads were washed with PBS and stored in 100 μl of QBS buffer (PBS containing 1% BSA and 0.02% sodium azide). .. To assess KAMPs binding to TLR4/MD-2, TLR4/MD-2 complex-conjugated beads (5,000 in FACS buffer) were preincubated with KAMP-10 (48 μg/ml), KAMP-18C (96 μg/ml) or SC-10 (48 μg/ml) in the presence or absence of recombinant human MD-2 (R&D) (1 μg/ml) for 1 h on ice. .. Beads were then washed twice with PBS before incubation with FITC-E. coli O55:B5 LPS (1 μg/ml) (Sigma-Aldrich) for 1 h on ice.

    Recombinant:

    Article Title: Simultaneous Control of Infection and Inflammation by Keratin-Derived Antibacterial Peptides (KAMPs) Targeting TLRs and Co-Receptors
    Article Snippet: One quarter of the bead suspension was mixed with 50 μl of PBS containing 25 μg of recombinant human TLR4/MD-2 complex or TLR2 (R&D) for 3 hours at 25 ° C. Following conjugation, beads were washed with PBS and stored in 100 μl of QBS buffer (PBS containing 1% BSA and 0.02% sodium azide). .. To assess KAMPs binding to TLR4/MD-2, TLR4/MD-2 complex-conjugated beads (5,000 in FACS buffer) were preincubated with KAMP-10 (48 μg/ml), KAMP-18C (96 μg/ml) or SC-10 (48 μg/ml) in the presence or absence of recombinant human MD-2 (R&D) (1 μg/ml) for 1 h on ice. .. Beads were then washed twice with PBS before incubation with FITC-E. coli O55:B5 LPS (1 μg/ml) (Sigma-Aldrich) for 1 h on ice.

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    Clear Native PAGE:

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    In Vitro:

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    Sonication:

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    Incubation:

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    Article Title: The matricellular protein SPARC induces inflammatory interferon-response in macrophages during aging.
    Article Snippet: .. Nunc Maxisorp 96-well plates (Thermo Fischer Scientific) were coated with 100 mL solution containing 0.25, 2.5, and 25 mg/mL of each hTLR4 (R&D), hTLR2 (R&D), human MD-2 (R&D), mTLR4 (CUSABIO), and BSA (Bio-Rad) in PBS and incubated overnight at 4 C. After washing with washing buffer (PBST, Tween 20 0.05%) three times, unspecific binding was blocked with 10% BSA in PBST (0.05% Tween 20) for 1 h at room temperature. .. Following three times of washing, 20 mg/mL SPARC recombinant proteins (Peprotech) were added in 2% BSA/PBST, incubated for 2 h at room temperature, and washed three times.

    Western Blot:

    Article Title: Zhankuic Acid A Isolated from Taiwanofungus camphoratus Is a Novel Selective TLR4/MD-2 Antagonist with Anti-Inflammatory Properties
    Article Snippet: .. Native PAGE For in vitro binding analysis, predetermined amounts of LPS or ZAA were sonicated for 3 min and incubated with recombinant human MD-2 (R&D Systems, Minneapolis, MN; 0.15 μg) or recombinant human TLR4/MD-2 complex (R&D Systems; 1 μg) at 37°C for 3 h. Samples were subjected to native PAGE, and the levels of TLR4-associated or free MD-2 were detected by immunoblotting with two anti–MD-2 Abs, rabbit polyclonal Ab against MD-2 aas 110–160 (Abcam, Cambridge, MA) and mouse mAb against MD-2 aas 2–160 (Abcam). ..

    other:

    Article Title: MD-2 is required for disulfide HMGB1–dependent TLR4 signaling
    Article Snippet: Human TLR4–MD-2 complex, human MD-2, TLR2, and soluble RAGE were obtained from R&D Systems.



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    Image Search Results


    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.

    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

    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.

    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

    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.

    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

    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.

    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

    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.

    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

    ( A ) Detection of HMGB1 in CM from a panel of prostate cancer (CaP) cell lines, including LNCaP control (PCMV vector) and MD2-overexpressing cells (M2 vector). ( B ) HMGB1 levels in CM from DU145 control cells (SCR-siRNA) and MD2-silenced cells (MD2 siRNA). ( C ) Levels of soluble MD2 (sMD2) and HMGB1 in CM from LNCaP cells overexpressing MD2 after treatment with the MD2 inhibitor (MD2-int-1) or vehicle control for 24 h.

    Journal: Oncoscience

    Article Title: Targeting MD2 in prostate cancer bone metastasis: Mechanistic insights and therapeutic potential

    doi: 10.18632/oncoscience.647

    Figure Lengend Snippet: ( A ) Detection of HMGB1 in CM from a panel of prostate cancer (CaP) cell lines, including LNCaP control (PCMV vector) and MD2-overexpressing cells (M2 vector). ( B ) HMGB1 levels in CM from DU145 control cells (SCR-siRNA) and MD2-silenced cells (MD2 siRNA). ( C ) Levels of soluble MD2 (sMD2) and HMGB1 in CM from LNCaP cells overexpressing MD2 after treatment with the MD2 inhibitor (MD2-int-1) or vehicle control for 24 h.

    Article Snippet: Once tumors were established, as confirmed by IVIS bioluminescence imaging, mice were randomized to receive either vehicle or the selective small molecule MD2 inhibitor, MD2-int-1 (MedChemExpress), for three weeks.

    Techniques: Control, Plasmid Preparation