BMP2 Antibody - #AF5163

Fig. 6 The ERK and BMP2 signaling pathway is activated by high extracellular Mg2+ in DPSCs during odontogenic differentiation. a ERK phosphorylation was significantly enhanced in DPSCs treated with 1 mM, 5 mM, and 10 mM Mg2+ compared with the 0 mM Mg2+ group, but p38 and JNK phosphorylation amounts were unchanged. b ERK phosphorylation was reduced by 2-APB. c Consistently, the protein levels of BMP2, BMPR1, and phosphorylated Smad1/5/9 were significantly increased in DPSCs exposed to high extracellular Mg2+. d BMP2, BMPR1, and phosphorylated Smad1/5/9 protein amounts were decreased by 2-APB

FIGURE 4 In (A), the immunohistochemical results of Piezo1, RUNX2, BMP2, CD31, HIF-a, and VEGF are presented. Additionally, (B–G) display the corresponding quantitative immunohistochemical results. In comparison to the model group, both the blank and WBVT groups exhibited significantly higher expression levels of Piezo1, RUNX2, BMP2, CD31, HIF-a, and VEGF. These differences were statistically significant (p < 0.05).

Figure 3 miR-129-5p promoted osteoblast differentiation of BMSCs. BMSCs were transduced with a lentiviral vector containing miR-129-5p mimic, miR-129-5p inhibitor, or negative control (NC) lentivirus, respectively. 48 hours after transduction, cells were cultured in osteoblast induction medium. ALP staining was performed at days 7 and 14 following induction (a); corresponding ALP absorbance index was calculated (b). ARS staining of BMSCs was performed at days 14 and 21 following induction (c); corresponding ARS absorbance index was calculated (d). mRNA (e) and protein (f) levels of osteoblast-related genes Runx2, Bmp2, and OCN were detected by quantitative RT-PCR and western blot, respectively. β-Actin was used as an internal control. All data were expressed as means ± SD. ∗p < 0.05 and ∗∗p < 0.01.

FIGURE 6 |Effects of ITE on the expression of TGF‐β1, BMP2 and BMP9 in HPAECs induced by hypoxia. HPAECs were cultured under the conditions of normoxia, normoxia + ITE, hypoxia and hypoxia + ITE, respectively. *P < 0.05, **P < 0.01, and ***P < 0.001. BMP, bone morphogenetic protein; HPAEC, human pulmonary arterial endothelial cell; ITE, 2‐(1′H‐indole‐3′‐carbonyl)‐thiazole‐4‐carboxylicacid methyl ester; TGF‐β, transforming growth factor‐β

Fig. 2. Comparison of osteogenic differentiation ability between NC and DOP(diabetic osteoporosis) hJBMMSCs. A. The ALP staining area was smaller and the color was lighter in DOP group than NC group on the 10th day (Mean ± SD, n = 6). B. The ALP activity was lower in DOP group than NC group after 7 days and 14 days of osteogenic induction (Mean ± SD, n = 6). C. After osteogenic induction, ARS (alizarin red S) staining on the 21st day showed that the number of mineralized nodules in DOP group was significantly less than that in NC group (Mean ± SD, n = 6). D. semiquantitative analysis showed that the OD (optical density) value of DOP group was significantly lower than that of NC group (Mean ± SD, n = 6). E. After osteogenic induction, the mRNA expressions of RUNX2, BMP2,ALP, OCN, SP7 and DLX5 in DOP group were significantly lower than those in NC group (Mean ± SD, n = 3). F. The protein expressions of RUNX2, BMP2, ALP and DLX5 in DOP group were significantly lower than those in NC group (Mean ± SD, n = 3). **P < 0.01,***P < 0.001.

Fig. 2. Emo stimulates bone formation in the rats of the OP-OA group. (A) Molecular formula of Emo. (B, C) Immunoblot analysis of RUNX2, BMP2, and OCN. (D) Real-time PCR results of RUNX2, BMP2, and OCN. Data are expressed as mean ± standard deviation. ns, not significant