tfiid antibody Search Results


anti tbp  (Proteintech)
93
Proteintech anti tbp
Anti Tbp, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tfiid  (Santa Cruz Biotechnology)
94
Santa Cruz Biotechnology tfiid
Tfiid, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tbp proteintech  (Proteintech)
93
Proteintech tbp proteintech
Figure 5. The p90aDMA and p70aDMA proteins accumulate in the nucleus of cancer cells and degrade in response to cellular stresses. (A) Nuclear and cytoplasmic extracts were prepared after MDA-MB‑231 cells were cultured with IL-2 or IL-6 as indicated. Fractions were analyzed by western blot analysis using antibody to ASYM24. <t>TBP</t> was probed as a loading control. (B and C) MDA-MB‑231 cells or HeLa cells were cultured under normoxic (21% O2) or hypoxic (1% O2) conditions for 24 h. (D) HeLa cells were cultured in HBSS medium for 24 h to induce autophagy or left in the complete culture medium. The cells were harvested and nuclear and cytoplasmic extracts were prepared for western blot analysis using antibodies to LC3 and ASYM24, respectively. Fractionation efficiency was determined by localization <t>of</t> <t>β-actin</t> (cytoplasm) and TBP (nucleus).
Tbp Proteintech, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/tbp proteintech/product/Proteintech
Average 93 stars, based on 1 article reviews
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emerin antibody  (Proteintech)
91
Proteintech emerin antibody
Figure 5. The p90aDMA and p70aDMA proteins accumulate in the nucleus of cancer cells and degrade in response to cellular stresses. (A) Nuclear and cytoplasmic extracts were prepared after MDA-MB‑231 cells were cultured with IL-2 or IL-6 as indicated. Fractions were analyzed by western blot analysis using antibody to ASYM24. <t>TBP</t> was probed as a loading control. (B and C) MDA-MB‑231 cells or HeLa cells were cultured under normoxic (21% O2) or hypoxic (1% O2) conditions for 24 h. (D) HeLa cells were cultured in HBSS medium for 24 h to induce autophagy or left in the complete culture medium. The cells were harvested and nuclear and cytoplasmic extracts were prepared for western blot analysis using antibodies to LC3 and ASYM24, respectively. Fractionation efficiency was determined by localization <t>of</t> <t>β-actin</t> (cytoplasm) and TBP (nucleus).
Emerin Antibody, supplied by Proteintech, 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/emerin antibody/product/Proteintech
Average 91 stars, based on 1 article reviews
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tbp antibodies  (Boster Bio)
90
Boster Bio tbp antibodies
Figure 5. The p90aDMA and p70aDMA proteins accumulate in the nucleus of cancer cells and degrade in response to cellular stresses. (A) Nuclear and cytoplasmic extracts were prepared after MDA-MB‑231 cells were cultured with IL-2 or IL-6 as indicated. Fractions were analyzed by western blot analysis using antibody to ASYM24. <t>TBP</t> was probed as a loading control. (B and C) MDA-MB‑231 cells or HeLa cells were cultured under normoxic (21% O2) or hypoxic (1% O2) conditions for 24 h. (D) HeLa cells were cultured in HBSS medium for 24 h to induce autophagy or left in the complete culture medium. The cells were harvested and nuclear and cytoplasmic extracts were prepared for western blot analysis using antibodies to LC3 and ASYM24, respectively. Fractionation efficiency was determined by localization <t>of</t> <t>β-actin</t> (cytoplasm) and TBP (nucleus).
Tbp Antibodies, supplied by Boster Bio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tbp  (Boster Bio)
93
Boster Bio tbp
Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 <t>and</t> <t>β-catenin.</t> Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and <t>TBP</t> in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.
Tbp, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
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anti tata binding protein tbp  (Proteintech)
91
Proteintech anti tata binding protein tbp
Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 <t>and</t> <t>β-catenin.</t> Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and <t>TBP</t> in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.
Anti Tata Binding Protein Tbp, supplied by Proteintech, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 91 stars, based on 1 article reviews
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taf11  (Proteintech)
93
Proteintech taf11
Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 <t>and</t> <t>β-catenin.</t> Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and <t>TBP</t> in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.
Taf11, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-tfiid antibody  (Upstate Biotechnology Inc)
90
Upstate Biotechnology Inc anti-tfiid antibody
Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 <t>and</t> <t>β-catenin.</t> Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and <t>TBP</t> in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.
Anti Tfiid Antibody, supplied by Upstate Biotechnology 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/anti-tfiid antibody/product/Upstate Biotechnology Inc
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antibodies against tnfrsf1a, tnfrsf1b and transcription factor ii d (tfiid)  (Wanleibio)
90
Wanleibio antibodies against tnfrsf1a, tnfrsf1b and transcription factor ii d (tfiid)
Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 <t>and</t> <t>β-catenin.</t> Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and <t>TBP</t> in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.
Antibodies Against Tnfrsf1a, Tnfrsf1b And Transcription Factor Ii D (Tfiid), 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
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Image Search Results


Figure 5. The p90aDMA and p70aDMA proteins accumulate in the nucleus of cancer cells and degrade in response to cellular stresses. (A) Nuclear and cytoplasmic extracts were prepared after MDA-MB‑231 cells were cultured with IL-2 or IL-6 as indicated. Fractions were analyzed by western blot analysis using antibody to ASYM24. TBP was probed as a loading control. (B and C) MDA-MB‑231 cells or HeLa cells were cultured under normoxic (21% O2) or hypoxic (1% O2) conditions for 24 h. (D) HeLa cells were cultured in HBSS medium for 24 h to induce autophagy or left in the complete culture medium. The cells were harvested and nuclear and cytoplasmic extracts were prepared for western blot analysis using antibodies to LC3 and ASYM24, respectively. Fractionation efficiency was determined by localization of β-actin (cytoplasm) and TBP (nucleus).

Journal: International journal of oncology

Article Title: An asymmetrically dimethylarginated nuclear 90 kDa protein (p90aDMA) induced by interleukin (IL)-2, IL-4 or IL-6 in the tumor microenvironment is selectively degraded by autophagy.

doi: 10.3892/ijo.2016.3450

Figure Lengend Snippet: Figure 5. The p90aDMA and p70aDMA proteins accumulate in the nucleus of cancer cells and degrade in response to cellular stresses. (A) Nuclear and cytoplasmic extracts were prepared after MDA-MB‑231 cells were cultured with IL-2 or IL-6 as indicated. Fractions were analyzed by western blot analysis using antibody to ASYM24. TBP was probed as a loading control. (B and C) MDA-MB‑231 cells or HeLa cells were cultured under normoxic (21% O2) or hypoxic (1% O2) conditions for 24 h. (D) HeLa cells were cultured in HBSS medium for 24 h to induce autophagy or left in the complete culture medium. The cells were harvested and nuclear and cytoplasmic extracts were prepared for western blot analysis using antibodies to LC3 and ASYM24, respectively. Fractionation efficiency was determined by localization of β-actin (cytoplasm) and TBP (nucleus).

Article Snippet: Target Source Host Dilution Catalog SYM11 Merck Millipore, MA, USA Rabbit 1:1,000 07-413 ASYM24 Merck Millipore, MA, USA Rabbit 1:500 07-414 LC3B Cell Signaling Technology, Inc. (CST), MA, USA Rabbit 1:1,000 #3868 ATG5 Cell Signaling Technology, Inc. (CST), MA, USA Rabbit 1:1,000 #12994 TBP Proteintech, Wu Han, China Rabbit 1:500 22006-1-AP β-actin Zen Bioscience, Cheng Du, China Mouse 1:20,000 70068 that were significantly reduced regardless of the interleukin stimulation (Fig. 2).

Techniques: Cell Culture, Western Blot, Control, Fractionation

Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 and β-catenin. Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and TBP in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.

Journal: Frontiers in Pharmacology

Article Title: Specnuezhenide Decreases Interleukin-1β-Induced Inflammation in Rat Chondrocytes and Reduces Joint Destruction in Osteoarthritic Rats

doi: 10.3389/fphar.2018.00700

Figure Lengend Snippet: Effect of SPN on IL-1β-induced nuclear translocation of NF-κB p65 and β-catenin. Nuclear and cytoplasmic extraction reagents were used to prepare nuclear (A) and cytoplasmic (B) extracts. Then, protein levels of β-catenin, NF-κB p65, GAPDH in the cytoplasm, and β-catenin, NF-κB p65, and TBP in the nucleus were assessed by Western blotting. GAPDH was used as an endogenous control in the cytoplasm, whereas TBP worked as an endogenous control in the nucleus ( n = 3 per group). (C) Chondrocytes were pretreated with SPN for 1 h, and then stimulated with IL-1β for 6 h for NF-κb-Luc activity analysis, or 12 h for TCF-LEF RE activity analysis ( n = 5 per group). Significance was calculated by one-way ANOVA with post hoc Tukey’s multiple comparisons test. ∗ p < 0.05, ∗∗∗ p < 0.001 versus the IL-1β+SPN (0 μM) group. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the NC group.

Article Snippet: In the present study, Ab against MMP-3 (rabbit mAb, Abcam, ab52915), MMP-9 (rabbit mAb, Abcam, ab76003), IL-6 (10E5, mouse mAb, Santa Cruz, sc-57315), iNOS (rabbit mAb, Abcam, ab3523), COX2 (D5H5, rabbit mAb, Cell Signaling, #12282), collagen 2 (rabbit mAb, Abcam, ab188570), sox9 (rabbit mAb, Abcam, ab185966), β-catenin (D10A8, rabbit mAb, Cell Signaling, #8480p), non-phospho (active) β-catenin (Ser45) (D2U8Y, rabbit mAb, Cell Signaling, #19807S), NF-κB p65 (C22B4, rabbit mAb, Cell Signaling, #4764S), phosphor-NF-κB p65 (Ser536) (rabbit Ab, Cell Signaling, #3031), β-actin (mouse mAb, Abcam, ab8226), GAPDH (rabbit mAb, Cell Signaling, #5174), and TBP (rabbit Ab, Bosterbio, BA3586-2) were used.

Techniques: Translocation Assay, Extraction, Western Blot, Control, Activity Assay