anti runx2 rabbit polyclonal  (Novus Biologicals)

Journal: The Journal of thoracic and cardiovascular surgery

Article Title: Bone morphogenic protein 2 induces Runx2 and osteopontin expression in human aortic valve interstitial cells: role of Smad1 and extracellular signal-regulated kinase 1/2.

doi: 10.1016/j.jtcvs.2009.06.024

Figure Lengend Snippet: FIGURE 2. Bone morphogenic protein 2 (BMP-2) induces Runx2 and osteo- pontin expression in interstitial cells. A, Representative immunoblot shows that BMP-2 stimulation induced Runx2 expression at 24 hours, and cellular Runx2 level increased further with 48 hours of stimulation. B, Osteopontin levels in- creased in interstitial cells stimulated with BMP-2 for 48 hours in comparison with those seen in control (Ctrl; untreated) cells. C, Densitometric data show thatbothRunx2andosteopontinlevelsaresignificantlyincreasedafter48hours of BMP-2 stimulation. Data are expressed as means standard errors (n ¼ 3). *P<.05 versus control.

Article Snippet: Rabbit polyclonal antibody against Runx2 was purchased from Novus Biologicals (Littleton, Colo).

Techniques: Expressing, Western Blot, Comparison, Control

Journal: The Journal of thoracic and cardiovascular surgery

Article Title: Bone morphogenic protein 2 induces Runx2 and osteopontin expression in human aortic valve interstitial cells: role of Smad1 and extracellular signal-regulated kinase 1/2.

doi: 10.1016/j.jtcvs.2009.06.024

Figure Lengend Snippet: FIGURE 4. Silencing Smad1 reduces the expression of both Runx2 and osteopontin after bone morphogenic protein 2 (BMP-2) stimulation, whereas in- hibiting extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylation only reduces expression of osteopontin. A, Treatment with Smad1 small inter- fering RNA (siRNA) at concentrations of 60 and 90 nmol/L reduced cellular Smad1 levels by 25% and 51%, respectively. B, Pretreatment of cells with Smad1 siRNA at 90 nmol/L reduced Runx2 and osteopontin levels after 48 hours of BMP-2 stimulation. C, Densitometric data show that silencing Smad1 reduced BMP-2–induced expression of Runx2 and osteopontin by 54% and 46%, respectively. Data are expressed as means standard errors (n ¼ 3). *P<.05 versus untreated control and scrambled RNA control. D, Treatment with PD 98059 (PD; 25 mmol/L) markedly reduced ERK1/2 phosphorylation induced by BMP-2, whereas vehicle dimethyl sulfoxide (DMSO) had no effect. GAPDH, Glyceraldehyde-3-phosphate dehydrogenase. E, Inhibition of ERK1/2 had no effect on BMP-2–induced Runx2 expression. In contrast, it reduced cellular osteopontin level after BMP-2 stimulation. F, Densitometric data show that inhibition of ERK1/2 reduced BMP-2–induced osteopontin expression by 76%. Data are expressed as means standard errors (n ¼ 3). *P<.05 versus untreated control and DMSO control.

Article Snippet: Rabbit polyclonal antibody against Runx2 was purchased from Novus Biologicals (Littleton, Colo).

Techniques: Expressing, Phospho-proteomics, Control, Inhibition