bnip3 rodent Search Results


96
Cell Signaling Technology Inc rodent bnip3
Figure 3 <t>BNIP3</t> governs glutamine-driven malignant traits of melanoma cells.
Rodent Bnip3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rodent bnip3/product/Cell Signaling Technology Inc
Average 96 stars, based on 1 article reviews
rodent bnip3 - by Bioz Stars, 2026-05
96/100 stars
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91
Novus Biologicals bnip3 rodent
Figure 3. <t>BNIP3</t> enhances mt-reactive oxygen species production, and attenuates mt-membrane
Bnip3 Rodent, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/bnip3 rodent/product/Novus Biologicals
Average 91 stars, based on 1 article reviews
bnip3 rodent - by Bioz Stars, 2026-05
91/100 stars
  Buy from Supplier

Image Search Results


Figure 3 BNIP3 governs glutamine-driven malignant traits of melanoma cells.

Journal: Biological chemistry

Article Title: BNIP3 contributes to the glutamine-driven aggressive behavior of melanoma cells.

doi: 10.1515/hsz-2018-0208

Figure Lengend Snippet: Figure 3 BNIP3 governs glutamine-driven malignant traits of melanoma cells.

Article Snippet: Incubation with primary antibodies [HIF1α (Cayman Chemical, Ann Arbor, USA), rodent BNIP3 (Cell Signaling Technologies, Danvers, USA), human BNIP3 (Sigma Aldrich Protein Atlas), Twist (Active Motif, La Hulpe, Belgium) and actin (Sigma Aldrich)] was performed overnight at 4oC.

Techniques:

Figure 3. BNIP3 enhances mt-reactive oxygen species production, and attenuates mt-membrane

Journal: Cells

Article Title: Multiomics Approach Reveals an Important Role of BNIP3 in Myocardial Remodeling and the Pathogenesis of Heart Failure with Reduced Ejection Fraction.

doi: 10.3390/cells11091572

Figure Lengend Snippet: Figure 3. BNIP3 enhances mt-reactive oxygen species production, and attenuates mt-membrane

Article Snippet: The following primary antibodies were used: total OXPHOS rodent antibody cocktail, HADHA, HADHB, MCAD, VDAC1, SLC25A4, SLC25A5, SLC25A11 (Abcam, Boston, MA, USA); BNIP3 rodent specific, GAPDH, AMPKα, p-S485/491-AMPKα, p-T197-AMPKα, GSK3α, p-S21-GSK3α, GSK3β, p-S9-GSK3β, TNNI3, p-S23/24-TNNI3, and PP1a (Cell signaling, Danvers, MA, USA); PGC1α (Novus Biologicals, Centennial, CO, USA); LETM1 (Proteintech, Rosemont, IL, USA); SERCA2A, PLN, and p-S16-PLN (Badrilla, Leeds, UK).

Techniques: Membrane

Figure 7. BNIP3 interactome in human and rat LV myocardia identified via BNIP3 co- immunoprecipitation (Co-IP) and mass spectrometry. (A). Venn diagrams show the total number of identified BNIP3 interacting proteins by mass spectrometry in the human (red) and rat (green) HFrEF LV myocardium. The intersection between the two Venn diagrams (black circle) shows the number of commonly identified BNIP3 interacting proteins in human and rat samples. (B,C). Heat maps and PCA plots show the relative log2-fold expression and the variance in biological samples, respectively, in Sham and HFrEF in the rat LV myocardium of the 516 common identified BNIP3 interacting proteins (left), including those that were differentially expressed in HFrEF vs. Sham, taking a cutoff p-value of < 0.05 (right). (D). Heat maps show the relative log2-fold expression in Sham and HFrEF in the rat LV myocardium of some of the important identified BNIP3 interacting proteins that were commonly identified in rat and human HFrEF samples, presented by HFrEF vs. Sham cutoff p-value < 0.05 (left), 0.05 < p < 0.1 (middle), and p > 0.1 (right). (E). Western blot showing the expression of sarco/endoplasmic reticulum calcium ATPase 2a (SERCA2a) and the mt-proton/calcium exchanger protein (LETM1) in Sham, ShLuc, and ShBNIP3, * p < 0.05 vs. Sham and † p < 0.05 vs. ShLuc; m, monomer; t, trimer. (F,G). Heat maps of the top Canonical Pathways and Upstream Regulators that were

Journal: Cells

Article Title: Multiomics Approach Reveals an Important Role of BNIP3 in Myocardial Remodeling and the Pathogenesis of Heart Failure with Reduced Ejection Fraction.

doi: 10.3390/cells11091572

Figure Lengend Snippet: Figure 7. BNIP3 interactome in human and rat LV myocardia identified via BNIP3 co- immunoprecipitation (Co-IP) and mass spectrometry. (A). Venn diagrams show the total number of identified BNIP3 interacting proteins by mass spectrometry in the human (red) and rat (green) HFrEF LV myocardium. The intersection between the two Venn diagrams (black circle) shows the number of commonly identified BNIP3 interacting proteins in human and rat samples. (B,C). Heat maps and PCA plots show the relative log2-fold expression and the variance in biological samples, respectively, in Sham and HFrEF in the rat LV myocardium of the 516 common identified BNIP3 interacting proteins (left), including those that were differentially expressed in HFrEF vs. Sham, taking a cutoff p-value of < 0.05 (right). (D). Heat maps show the relative log2-fold expression in Sham and HFrEF in the rat LV myocardium of some of the important identified BNIP3 interacting proteins that were commonly identified in rat and human HFrEF samples, presented by HFrEF vs. Sham cutoff p-value < 0.05 (left), 0.05 < p < 0.1 (middle), and p > 0.1 (right). (E). Western blot showing the expression of sarco/endoplasmic reticulum calcium ATPase 2a (SERCA2a) and the mt-proton/calcium exchanger protein (LETM1) in Sham, ShLuc, and ShBNIP3, * p < 0.05 vs. Sham and † p < 0.05 vs. ShLuc; m, monomer; t, trimer. (F,G). Heat maps of the top Canonical Pathways and Upstream Regulators that were

Article Snippet: The following primary antibodies were used: total OXPHOS rodent antibody cocktail, HADHA, HADHB, MCAD, VDAC1, SLC25A4, SLC25A5, SLC25A11 (Abcam, Boston, MA, USA); BNIP3 rodent specific, GAPDH, AMPKα, p-S485/491-AMPKα, p-T197-AMPKα, GSK3α, p-S21-GSK3α, GSK3β, p-S9-GSK3β, TNNI3, p-S23/24-TNNI3, and PP1a (Cell signaling, Danvers, MA, USA); PGC1α (Novus Biologicals, Centennial, CO, USA); LETM1 (Proteintech, Rosemont, IL, USA); SERCA2A, PLN, and p-S16-PLN (Badrilla, Leeds, UK).

Techniques: Immunoprecipitation, Co-Immunoprecipitation Assay, Mass Spectrometry, Expressing, Western Blot

Figure 8. Schematic drawings highlight some of the key findings of the effect of BNIP3 knockdown in the rat pressure overload HFrEF model. These are presented as ShL vs. Sham (A) and ShB vs. ShL (B). The green and red color intensities show the degree of downregulation and upregulation of activity, respectively, or the log2-fold change in protein or phosphosite expression, as noted by the scale bar at the bottom right side of the schematic drawing. The double-headed arrows show the interaction between BNIP3 and its interacting protein. The blue and orange colors show whether there was inhibition/downregulation or activation/upregulation as a result of this interaction. The straight black arrows point to an effect of BNIP3 on protein phosphorylation. The black asterisk denotes

Journal: Cells

Article Title: Multiomics Approach Reveals an Important Role of BNIP3 in Myocardial Remodeling and the Pathogenesis of Heart Failure with Reduced Ejection Fraction.

doi: 10.3390/cells11091572

Figure Lengend Snippet: Figure 8. Schematic drawings highlight some of the key findings of the effect of BNIP3 knockdown in the rat pressure overload HFrEF model. These are presented as ShL vs. Sham (A) and ShB vs. ShL (B). The green and red color intensities show the degree of downregulation and upregulation of activity, respectively, or the log2-fold change in protein or phosphosite expression, as noted by the scale bar at the bottom right side of the schematic drawing. The double-headed arrows show the interaction between BNIP3 and its interacting protein. The blue and orange colors show whether there was inhibition/downregulation or activation/upregulation as a result of this interaction. The straight black arrows point to an effect of BNIP3 on protein phosphorylation. The black asterisk denotes

Article Snippet: The following primary antibodies were used: total OXPHOS rodent antibody cocktail, HADHA, HADHB, MCAD, VDAC1, SLC25A4, SLC25A5, SLC25A11 (Abcam, Boston, MA, USA); BNIP3 rodent specific, GAPDH, AMPKα, p-S485/491-AMPKα, p-T197-AMPKα, GSK3α, p-S21-GSK3α, GSK3β, p-S9-GSK3β, TNNI3, p-S23/24-TNNI3, and PP1a (Cell signaling, Danvers, MA, USA); PGC1α (Novus Biologicals, Centennial, CO, USA); LETM1 (Proteintech, Rosemont, IL, USA); SERCA2A, PLN, and p-S16-PLN (Badrilla, Leeds, UK).

Techniques: Knockdown, Activity Assay, Phospho-proteomics, Expressing, Inhibition, Activation Assay