rabbit primary antibody against a sma Search Results


antibodies to extracellular signal regulated kinase 1/2 (erk1/2)  (Wanleibio)
90
Wanleibio antibodies to extracellular signal regulated kinase 1/2 (erk1/2)
JNK activation contributes to ZnO NPs-induced PC12 cell death. Effects of ZnO NPs on <t>p38,</t> ERK (a) , and JNK (b) signaling pathways. Activation status of the p38, ERK, and JNK was analyzed in whole cell proteins by immunoblotting with antibodies to phosphorylated p38, ERK, JNK and total p38, ERK, JNK, respectively. The densitometry of those bolts from at least three independent experiments was shown in Figure C and D. Effect of JNK, p38 and ERK inhibitors on ZnO NPs-induced cell death as shown by PI staining (c) and CCK8 assay (d) . Cells were pretreated with 10 μM JNK inhibitor SP600125, 3 μM p38 inhibitor SB203580 and 10 μM ERK inhibitor PD98059 for 1 h, followed by exposure to 15 μg/mL ZnO NPs for 12 h. Data from at least three independent experiments were expressed as the means ± SD. *** p < 0.001 compared with the untreated control
Antibodies To Extracellular Signal Regulated Kinase 1/2 (Erk1/2), supplied by Wanleibio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/antibodies to extracellular signal regulated kinase 1/2 (erk1/2)/product/Wanleibio
Average 90 stars, based on 1 article reviews
antibodies to extracellular signal regulated kinase 1/2 (erk1/2) - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
rabbit primary antibodies generated against a synthetic ovine -end bound to keyhole limpet hemocyanin  (ICN Biomedicals)
90
ICN Biomedicals rabbit primary antibodies generated against a synthetic ovine -end bound to keyhole limpet hemocyanin
JNK activation contributes to ZnO NPs-induced PC12 cell death. Effects of ZnO NPs on <t>p38,</t> ERK (a) , and JNK (b) signaling pathways. Activation status of the p38, ERK, and JNK was analyzed in whole cell proteins by immunoblotting with antibodies to phosphorylated p38, ERK, JNK and total p38, ERK, JNK, respectively. The densitometry of those bolts from at least three independent experiments was shown in Figure C and D. Effect of JNK, p38 and ERK inhibitors on ZnO NPs-induced cell death as shown by PI staining (c) and CCK8 assay (d) . Cells were pretreated with 10 μM JNK inhibitor SP600125, 3 μM p38 inhibitor SB203580 and 10 μM ERK inhibitor PD98059 for 1 h, followed by exposure to 15 μg/mL ZnO NPs for 12 h. Data from at least three independent experiments were expressed as the means ± SD. *** p < 0.001 compared with the untreated control
Rabbit Primary Antibodies Generated Against A Synthetic Ovine End Bound To Keyhole Limpet Hemocyanin, supplied by ICN Biomedicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit primary antibodies generated against a synthetic ovine -end bound to keyhole limpet hemocyanin/product/ICN Biomedicals
Average 90 stars, based on 1 article reviews
rabbit primary antibodies generated against a synthetic ovine -end bound to keyhole limpet hemocyanin - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
primary antibody raised in rabbit against a conserved region of the human fos ab5  (Oncogene Science Inc)
90
Oncogene Science Inc primary antibody raised in rabbit against a conserved region of the human fos ab5
JNK activation contributes to ZnO NPs-induced PC12 cell death. Effects of ZnO NPs on <t>p38,</t> ERK (a) , and JNK (b) signaling pathways. Activation status of the p38, ERK, and JNK was analyzed in whole cell proteins by immunoblotting with antibodies to phosphorylated p38, ERK, JNK and total p38, ERK, JNK, respectively. The densitometry of those bolts from at least three independent experiments was shown in Figure C and D. Effect of JNK, p38 and ERK inhibitors on ZnO NPs-induced cell death as shown by PI staining (c) and CCK8 assay (d) . Cells were pretreated with 10 μM JNK inhibitor SP600125, 3 μM p38 inhibitor SB203580 and 10 μM ERK inhibitor PD98059 for 1 h, followed by exposure to 15 μg/mL ZnO NPs for 12 h. Data from at least three independent experiments were expressed as the means ± SD. *** p < 0.001 compared with the untreated control
Primary Antibody Raised In Rabbit Against A Conserved Region Of The Human Fos Ab5, supplied by Oncogene Science Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/primary antibody raised in rabbit against a conserved region of the human fos ab5/product/Oncogene Science Inc
Average 90 stars, based on 1 article reviews
primary antibody raised in rabbit against a conserved region of the human fos ab5 - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
the primary antibodies used in this study were raised in rabbit against a peptide sequence from the zfd of rela  (Kaneka Corp)
90
Kaneka Corp the primary antibodies used in this study were raised in rabbit against a peptide sequence from the zfd of rela
(A) Domain structure of <t>RelA,</t> the enzymatically-inactive (p)ppGpp hydrolysis (HD*) and a functional (p)ppGpp synthesis (SYNTH) NTD domains. TGS (ThrRS, GTPase and SpoT), <t>Helical,</t> <t>ZFD</t> (Zinc Finger Domain) and RRM (RNA recognition motif) domains comprise the regulatory CTD region. (B) E. coli MG1655 (wt) cells were transformed with high copy IPTG inducible vector, pMG25 (vector), pMG25:: relA CTD , pMG25:: RelA CTD-C612G , pMG25:: RelA CTD-D637R , and pMG25:: RelA CTD-C638F . The transformed cells were grown at 37 °C overnight in M9 minimal medium with 100 μg/ml ampicillin. Ten-fold serial dilutions were made and spotted onto LB agar (LBA) supplemented with 100 μg/ml ampicillin, as a loading control, and onto SMG plates supplemented with 100 μg/ml ampicillin and 1 mM IPTG to induce relA variant expression. (C) Representative audioradiogram of a PEI Cellulose TLC plate showing (p)ppGpp accumulation of E. coli MG1655 carrying pMG25 (vector) or pMG25:: relA CTD upon valine-induced isoleucine starvation. See Materials and Methods for more details. (D) Overnight cultures of E. coli MG1655 (wt) and MG1655Δ relA (Δ relA ) transformed with pMG25 (vector) or pMG25:: relA CTD , grown in LB with 100 μg/ml ampicillin. Ten-fold serial dilutions of were made and spotted onto LB agar supplemented with 1 mM IPTG.
The Primary Antibodies Used In This Study Were Raised In Rabbit Against A Peptide Sequence From The Zfd Of Rela, supplied by Kaneka Corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/the primary antibodies used in this study were raised in rabbit against a peptide sequence from the zfd of rela/product/Kaneka Corp
Average 90 stars, based on 1 article reviews
the primary antibodies used in this study were raised in rabbit against a peptide sequence from the zfd of rela - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


JNK activation contributes to ZnO NPs-induced PC12 cell death. Effects of ZnO NPs on p38, ERK (a) , and JNK (b) signaling pathways. Activation status of the p38, ERK, and JNK was analyzed in whole cell proteins by immunoblotting with antibodies to phosphorylated p38, ERK, JNK and total p38, ERK, JNK, respectively. The densitometry of those bolts from at least three independent experiments was shown in Figure C and D. Effect of JNK, p38 and ERK inhibitors on ZnO NPs-induced cell death as shown by PI staining (c) and CCK8 assay (d) . Cells were pretreated with 10 μM JNK inhibitor SP600125, 3 μM p38 inhibitor SB203580 and 10 μM ERK inhibitor PD98059 for 1 h, followed by exposure to 15 μg/mL ZnO NPs for 12 h. Data from at least three independent experiments were expressed as the means ± SD. *** p < 0.001 compared with the untreated control

Journal: Particle and Fibre Toxicology

Article Title: Zinc oxide nanoparticles effectively regulate autophagic cell death by activating autophagosome formation and interfering with their maturation

doi: 10.1186/s12989-020-00379-7

Figure Lengend Snippet: JNK activation contributes to ZnO NPs-induced PC12 cell death. Effects of ZnO NPs on p38, ERK (a) , and JNK (b) signaling pathways. Activation status of the p38, ERK, and JNK was analyzed in whole cell proteins by immunoblotting with antibodies to phosphorylated p38, ERK, JNK and total p38, ERK, JNK, respectively. The densitometry of those bolts from at least three independent experiments was shown in Figure C and D. Effect of JNK, p38 and ERK inhibitors on ZnO NPs-induced cell death as shown by PI staining (c) and CCK8 assay (d) . Cells were pretreated with 10 μM JNK inhibitor SP600125, 3 μM p38 inhibitor SB203580 and 10 μM ERK inhibitor PD98059 for 1 h, followed by exposure to 15 μg/mL ZnO NPs for 12 h. Data from at least three independent experiments were expressed as the means ± SD. *** p < 0.001 compared with the untreated control

Article Snippet: Antibodies to p38 mitogen activated protein kinase (p38), extracellular signal regulated kinase 1/2 (ERK1/2) and JNK were purchased from Wanleibio (Shenyang, China).

Techniques: Activation Assay, Protein-Protein interactions, Western Blot, Staining, CCK-8 Assay, Control

(A) Domain structure of RelA, the enzymatically-inactive (p)ppGpp hydrolysis (HD*) and a functional (p)ppGpp synthesis (SYNTH) NTD domains. TGS (ThrRS, GTPase and SpoT), Helical, ZFD (Zinc Finger Domain) and RRM (RNA recognition motif) domains comprise the regulatory CTD region. (B) E. coli MG1655 (wt) cells were transformed with high copy IPTG inducible vector, pMG25 (vector), pMG25:: relA CTD , pMG25:: RelA CTD-C612G , pMG25:: RelA CTD-D637R , and pMG25:: RelA CTD-C638F . The transformed cells were grown at 37 °C overnight in M9 minimal medium with 100 μg/ml ampicillin. Ten-fold serial dilutions were made and spotted onto LB agar (LBA) supplemented with 100 μg/ml ampicillin, as a loading control, and onto SMG plates supplemented with 100 μg/ml ampicillin and 1 mM IPTG to induce relA variant expression. (C) Representative audioradiogram of a PEI Cellulose TLC plate showing (p)ppGpp accumulation of E. coli MG1655 carrying pMG25 (vector) or pMG25:: relA CTD upon valine-induced isoleucine starvation. See Materials and Methods for more details. (D) Overnight cultures of E. coli MG1655 (wt) and MG1655Δ relA (Δ relA ) transformed with pMG25 (vector) or pMG25:: relA CTD , grown in LB with 100 μg/ml ampicillin. Ten-fold serial dilutions of were made and spotted onto LB agar supplemented with 1 mM IPTG.

Journal: bioRxiv

Article Title: Intramolecular interactions dominate the autoregulation of Escherichia coli stringent factor RelA

doi: 10.1101/680231

Figure Lengend Snippet: (A) Domain structure of RelA, the enzymatically-inactive (p)ppGpp hydrolysis (HD*) and a functional (p)ppGpp synthesis (SYNTH) NTD domains. TGS (ThrRS, GTPase and SpoT), Helical, ZFD (Zinc Finger Domain) and RRM (RNA recognition motif) domains comprise the regulatory CTD region. (B) E. coli MG1655 (wt) cells were transformed with high copy IPTG inducible vector, pMG25 (vector), pMG25:: relA CTD , pMG25:: RelA CTD-C612G , pMG25:: RelA CTD-D637R , and pMG25:: RelA CTD-C638F . The transformed cells were grown at 37 °C overnight in M9 minimal medium with 100 μg/ml ampicillin. Ten-fold serial dilutions were made and spotted onto LB agar (LBA) supplemented with 100 μg/ml ampicillin, as a loading control, and onto SMG plates supplemented with 100 μg/ml ampicillin and 1 mM IPTG to induce relA variant expression. (C) Representative audioradiogram of a PEI Cellulose TLC plate showing (p)ppGpp accumulation of E. coli MG1655 carrying pMG25 (vector) or pMG25:: relA CTD upon valine-induced isoleucine starvation. See Materials and Methods for more details. (D) Overnight cultures of E. coli MG1655 (wt) and MG1655Δ relA (Δ relA ) transformed with pMG25 (vector) or pMG25:: relA CTD , grown in LB with 100 μg/ml ampicillin. Ten-fold serial dilutions of were made and spotted onto LB agar supplemented with 1 mM IPTG.

Article Snippet: The primary antibodies used in this study were raised in rabbit against a peptide sequence from the ZFD of RelA (Eurogentec).

Techniques: Functional Assay, Transformation Assay, Plasmid Preparation, Variant Assay, Expressing