Smad1, affinity purified antibody, goat, 100 ug.
- Known as:
- Smad1, antigenic enriched (anti-), caprine, 100 ug.
- Catalog number:
- GT15219-100
- Product Quantity:
- 1
- Category:
- -
- Supplier:
- Neuromi
- Gene target:
- Smad1 affinity purified antibody goat 100 .
Related genes to: Smad1, affinity purified antibody, goat, 100 ug.
- Gene:
- SMAD1 NIH gene
- Name:
- SMAD family member 1
- Previous symbol:
- MADH1
- Synonyms:
- MADR1, JV4-1
- Chromosome:
- 4q31.21
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-15
- Date modifiied:
- 2015-09-02
Related products to: Smad1, affinity purified antibody, goat, 100 ug.
Related articles to: Smad1, affinity purified antibody, goat, 100 ug.
- Excessive administration of glucocorticoids leads to arterial involvement and induces osteonecrosis. Conventional biomaterial-based strategies aimed at direct vascularization have shown limited therapeutic efficacy, primarily due to pronounced heterogeneity of neovasculature and vascular mispatterning. Here, we report a semisynthetic sulfated chitosan (SCS) that, when combined with bone morphogenetic protein-2 (BMP-2), rapidly reconstructs arterialized vasculature (type H vessels and arterioles) within the deteriorated bone, thereby coupling active osteoprogenitor cells. SCS positively regulates BMP-2-induced hypertrophic chondrocytes, which in turn secrete endogenous vascular endothelial growth factor to mediate arterial neovascularization. Instead of directly enhancing the Smad1/5/8 signaling pathway, SCS mitigates the intrinsic chronic inflammatory process of bone deterioration, preventing inflammatory factors from disrupting cartilage-to-bone transformation. In an osteonecrosis model, the synergistic effect of SCS and BMP-2 sustainably improved the femoral head's internal circulation system, rather than merely delaying disease progression. Therefore, this bioactive polysaccharide combined with an osteogenic factor enables arterialized vascularization during endochondral ossification, representing a promising therapeutic strategy for the treatment of ischemia-associated bone homeostasis disruption. - Source: PubMed
Publication date: 2026/04/13
Zhang ShuangLiu YangDeng ShunshuGao ZehuaWang JingLiu Changsheng - Non-transfusion dependent β-thalassemia (NTDT) is characterized by ineffective erythropoiesis, suppression of hepcidin, and iron overload, which is a major cause of morbidity and mortality. Hepatic protease Tmprss6 regulates hepcidin by modulating BMP/Smad signaling. Suppression of Tmprss6 in the mouse model of NTDT (Th3 mice), increased hepcidin and improved disease outcomes, but similar benefits have not been reported in human trials. We hypothesized that the resistance to the effects of anti-TMPRSS6 treatment in patients with NTDT may be caused by high erythroferrone (ERFE) concentrations and more severe iron overload, both known to modulate BMP/Smad signaling in hepatocytes. We therefore examined how ERFE and iron overload modulate the effects of Tmprss6 antisense oligonucleotides (ASO) in mouse models.We treated ERFE-overexpressing Th3 mice (T-E(M)) and their littermates (wild-type, Th3, and Erfe-overexpressing E(M) mice) with Tmprss6 ASO or non-targeting ASO for 4 weeks. Tmprss6 ASO increased phospho-Smad1/5/8 and hepcidin levels, decreased splenomegaly, reduced extramedullary erythropoiesis and improved iron parameters in Th3 mice but not in T-E(M) mice, despite similar Tmprss6 decrease. To determine whether iron overload alone blunted the effects of Tmprss6 ASO, we assessed the responses of C57BL/6 mice after 10 mg of iron dextran or 5000 ppm high iron diet. Unlike iron-adequate mice, iron-overloaded mice already had high phospho-Smad and hepcidin, with no further increase after Tmprss6 ASO treatment, and no effect on erythroid or iron parameters.Higher ERFE concentrations and more severe iron overload may be responsible for diminished benefits of Tmprss6 ASO in human NTDT. - Source: PubMed
Publication date: 2026/04/09
Zhang VidaBarrett Terrance DNemeth ElizabetaGanz Tomas - Pulmonary arterial hypertension (PAH) is characterized by excessive pulmonary vasoconstriction and vascular remodelling, with mutations in bone morphogenetic protein receptor type 2 (BMPR2) being the most common genetic alteration associated with the disease. While inflammatory mediators like interleukin-6 (IL-6) and the iron-regulatory hormone hepcidin have been implicated in vascular remodelling, their interaction with BMPR2 signalling remains poorly understood. This study investigated how IL-6 and hepcidin influence BMPR2 expression and downstream signalling in human pulmonary arterial endothelial cells (hPAECs). Using qPCR and Western blot analyses, we demonstrated that both IL-6 and hepcidin significantly reduced BMPR2 mRNA and protein levels in hPAECs. Intriguingly, despite this reduction, SMAD1/5 phosphorylation remained active, suggesting compensatory signalling through alternative receptor complexes. Treatment with IL-6 and hepcidin upregulated inhibitors of differentiation (ID) protein expression, mimicking the effects observed with BMPR2 knockdown. These findings reveal a novel regulatory axis involving IL-6, hepcidin, and BMPR2 in PAH pathogenesis, where IL-6 and hepcidin promote vascular remodelling through both BMPR2-dependent and independent mechanisms. These results suggest that therapeutic strategies targeting this axis, particularly those aimed at rebalancing BMP/TGF-β signalling, may hold promise for treating PAH. - Source: PubMed
Publication date: 2026/04/05
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Publication date: 2026/04/07
Ye HuiYueShao Liang - Mammalian palates are composed of the anterior hard palate and the posterior soft palate. However, the correlation of the genesis, pattern formation, and morphogenesis between the hard and soft palates remains elusive. - Source: PubMed
Publication date: 2026/03/20
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