antibodies against phospho jak2 tyr1007 1008  (Cell Signaling Technology Inc)

Journal: Pharmaceutical Science Advances

Article Title: Fufang Huangbo Formula mitigates myeloproliferative neoplasms by activating p53/p21 signaling axis and inhibiting STAT3 and NF-κB signaling pathways

doi: 10.1016/j.pscia.2026.100121

Figure Lengend Snippet: FHF provided therapeutic benefit in JAK2 V617F -induced MPN mice. (A) Schematic diagram of the JAK2 V617F -driven MPN mice and therapeutic intervention. Transplantation donors of bone marrow cells expressing JAK2 V617F were treated with vehicle or FHF for 6 weeks. (B) RBC, HGB, and HCT counts in PB from indicated mice after treatment. N = 6 mice per group. (C) Results of flow cytometry analysis of TER119 + cells in bone marrow. (D) Spleen size and weight of indicated mice after FHF treatment. (E-G) Representative H&E staining of spleen, BM and lung.

Article Snippet: JAK2 V617F -floxed mice and Vav-Cre mice were obtained from the Jackson Laboratory.

Techniques: Transplantation Assay, Expressing, Flow Cytometry, Staining

Journal: Pharmaceutical Science Advances

Article Title: Fufang Huangbo Formula mitigates myeloproliferative neoplasms by activating p53/p21 signaling axis and inhibiting STAT3 and NF-κB signaling pathways

doi: 10.1016/j.pscia.2026.100121

Figure Lengend Snippet: Schematic illustration of FHF treatment for MPNs. FHF treatment inhibits the JAK2/STAT3 and NF-κB signaling pathways. This suppresses the expression of pro-inflammatory cytokines and cell proliferation. On the other hand, FHF promotes cellular senescence by activating the p53/p21 signaling pathway.

Article Snippet: JAK2 V617F -floxed mice and Vav-Cre mice were obtained from the Jackson Laboratory.

Techniques: Protein-Protein interactions, Expressing

Journal: Advanced Science

Article Title: Gut Microbiota‐Derived Indole‐3‐Acetaldehyde Contributes to the Disease‐Alleviating Effects of Kurarinone in Experimental Autoimmune Encephalomyelitis

doi: 10.1002/advs.78358

Figure Lengend Snippet: IAAld suppresses Th1 and Th17 cell differentiation in an AhR‐dependent manner by repressing JAK/STAT signaling. (A) KEGG pathway enrichment analysis of the intersectional targets of IAAld and MS. (B) In silico prediction of the binding interaction between IAAld and AhR by molecular docking. The calculated binding energy (BE) is −6.6 kcal/mol (inset: chemical structure of IAAld). (C,D) Flow cytometric quantification and representative plots of CD4 + IFNγ + (Th1) and CD4 + IL‑17A + (Th17) cells under in vitro differentiation conditions across PBS, IAAld (10 µM), and IAAld+siAhR (AhR knockdown by siRNA) groups ( n = 3 per group). (E) Immunofluorescence staining of AhR (green) in Th1 and Th17 cells of each group, and cell nuclei were stained with DAPI (blue). (F) Western blot analysis showing protein levels of AhR, p‑JAK2, JAK2, p‑STAT4, STAT4, p‑STAT3, STAT3, SOCS1, SOCS3, and GAPDH in Th1 (left) and Th17 (right) cells. (G) Quantitative analysis of AhR/GAPDH ratio, p‐JAK2/JAK2 ratio, p‐STAT4/STAT4 ratio, p‐STAT3/STAT3 ratio, SOCS1/GAPDH ratio and SOCS3/GAPDH ratio in each group ( n = 4 per group). Data are presented as mean ± SEM. * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: SDS loading buffer (Deeyeebio, 50053) was added to the cell lysis solution, and the proteins (30 μg/lane) were separated by SDS‐PAGE and transferred onto the PVDF membrane, and probed with primary antibodies against phospho‐JAK2 (Tyr1007/1008) (CST, 3771), JAK2 (CST, 3230), phospho‐STAT3 (Ser705) (CST, 9145), phospho‐STAT4 (Tyr693) (CST, 4134), STAT3 (Proteintech, 10253‐2‐ap), STAT4 (CST, 2653), SOCS1 (CST, 55313), SOCS3 (Proteintech, 14025‐1‐ap), and AhR (Proteintech, 67785‐1‐lg), followed by HRP‐conjugated secondary antibodies (Proteintech, SA00001‐1, SA00001‐2).

Techniques: Cell Differentiation, Analysis, In Silico, Binding Assay, Docking Assay, In Vitro, Knockdown, Immunofluorescence, Staining, Western Blot, Significance Assay

Journal: Advanced Science

Article Title: Gut Microbiota‐Derived Indole‐3‐Acetaldehyde Contributes to the Disease‐Alleviating Effects of Kurarinone in Experimental Autoimmune Encephalomyelitis

doi: 10.1002/advs.78358

Figure Lengend Snippet: Graphical abstract. Schematic diagram illustrating the molecular mechanism by which KU ameliorates EAE through the gut microbiota‐IAAld‐AhR axis. KU reshapes gut microbiota composition in EAE mice, specifically increasing the abundance of Akkermansia muciniphila . A. muciniphila facilitates intestinal production of indole‐3‐acetaldehyde (IAAld) and the latter crosses the intestinal barrier to enter peripheral circulation and CNS, where IAAld activates AhR and promotes its nuclear translocation in CD4 + T cells. Once in the nucleus, activated AhR upregulates SOCS1 and SOCS3 expression and suppresses phosphorylation of JAK2 and its downstream targets, STAT4 and STAT3. This cascade restrains CD4 + T cell differentiation into Th1 and Th17 subsets, ultimately mitigating CNS inflammation and demyelination in EAE mice.

Article Snippet: SDS loading buffer (Deeyeebio, 50053) was added to the cell lysis solution, and the proteins (30 μg/lane) were separated by SDS‐PAGE and transferred onto the PVDF membrane, and probed with primary antibodies against phospho‐JAK2 (Tyr1007/1008) (CST, 3771), JAK2 (CST, 3230), phospho‐STAT3 (Ser705) (CST, 9145), phospho‐STAT4 (Tyr693) (CST, 4134), STAT3 (Proteintech, 10253‐2‐ap), STAT4 (CST, 2653), SOCS1 (CST, 55313), SOCS3 (Proteintech, 14025‐1‐ap), and AhR (Proteintech, 67785‐1‐lg), followed by HRP‐conjugated secondary antibodies (Proteintech, SA00001‐1, SA00001‐2).

Techniques: Translocation Assay, Expressing, Phospho-proteomics, Cell Differentiation