p tak 1 Search Results


94
Novus Biologicals anti p tak1
Anti P Tak1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti p tak1/product/Novus Biologicals
Average 94 stars, based on 1 article reviews
anti p tak1 - by Bioz Stars, 2026-03
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90
Beyotime tgfβ-activated kinase 1 (tak1
Tgfβ Activated Kinase 1 (Tak1, supplied by Beyotime, 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/tgfβ-activated kinase 1 (tak1/product/Beyotime
Average 90 stars, based on 1 article reviews
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90
ImmunoWay Biotechnology Company p-tak1 antibody
NLRC5 regulates microglial activation via promoting phosphorylation of IKKα/β. ( A ) Representative Western blot image of p-IKKα/β, IKKα/β, p-IκB and IκB in BV2-shCtrl and BV2-sh Nlrc5 cells treated with LPS (10 ng/mL) for different times. Bars represent the relative fold change of p-IKKα/β to IKKα/β ( B ) and p-IκB to IκB ( C ) (n = 5 for each group). ( D ) Representative Western blot image of <t>p-TAK1</t> and TAK1 in BV2-shCtrl and BV2-sh Nlrc5 cells treated with LPS. ( E ) Bars represent the relative fold change of p-TAK1 to TAK1 (n = 5 for each group). ( F ) Anti-NLRC5 was used to precipitate IKKα/β from BV2-shCtrl and BV2-sh Nlrc5 cell extracts. P-IKKα/β and IKKα/β were subsequently determined by Western blot analysis. ( G ) Representative Western blot image of p-IKKα/β, IKKα/β, p-IκB and IκB in RAW264.7-shCtrl and RAW264.7-sh Nlrc5 cells treated with LPS. Bars represent the relative fold change of p-IKKα/β to IKKα/β. ( H ) and p-IκB to IκB ( I ) (n = 5 for each group). All data were presented as mean ± SEM (( B ), LPS: F (3, 32) = 11.51, p < 0.001; NLRC5: F (1, 32) = 15.95, p < 0.001; Interaction: F (3, 32) = 3.201, p < 0.05; ( C ), LPS: F (3, 32) = 8.843, p < 0.001; NLRC5: F (1, 32) = 9.209, p < 0.01; Interaction: F (3, 32) = 4.286, p < 0.05; ( E ), LPS: F (3, 32) = 5.683, p < 0.01; NLRC5: F (1, 32) = 0.3470, p = 0.5600; Interaction: F (3, 32) = 0.1702, p = 0.9157; ( H ), LPS: (3, 32) = 78.14, p < 0.001; NLRC5: F (1, 32) = 8.092, p < 0.01; Interaction: F (3, 32) = 6.471, p < 0.01; ( I) , LPS: (3, 32) = 47.36, p < 0.001; NLRC5: F (1, 32) = 6.760, p < 0.05; Interaction: F (3, 32) = 3.143, p < 0.05). A two-way ANOVA was used to determine the statistical significance of the two groups. * p ≤ 0.05, ** p ≤ 0.01, and *** p ≤ 0.001. ns: no significant difference. p-IKKα/β: phosphorylated IKKα/β; p-IκB: phosphorylated IκB; p-TAK1: phosphorylated TAK1.
P Tak1 Antibody, supplied by ImmunoWay Biotechnology Company, 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/p-tak1 antibody/product/ImmunoWay Biotechnology Company
Average 90 stars, based on 1 article reviews
p-tak1 antibody - by Bioz Stars, 2026-03
90/100 stars
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90
Affinity Biosciences rabbit anti phospho tak1
SHP‐1 negatively regulates kinase phosphorylation in LPS‐treated rMC‐1 cells. A, Effects of SHP‐1 overexpression on inflammatory signalling pathways. Blank‐rLV‐ and SHP‐1‐rLV‐ transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15 or 30 min, and Western blotting was performed to determine the phosphorylation status of <t>TAK1,</t> JNK and NF‐κB and the total protein levels of JNK and NF‐κB. B‐D, Quantitative analysis of pTAK1/β‐actin (B), pJNK/JNK (C) and pNF‐κB/NF‐κB (D). E, Effects of SHP‐1 knockdown on inflammatory signalling pathways. Blank‐rLV‐ and shRNA‐SHP‐1‐rLV‐transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15, or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. F‐H, Quantitative analysis of pTAK1/β‐actin (F), pJNK/JNK (G) and pNF‐κB/NF‐κB (H). Two‐way ANOVA followed by Dunnett's test was used. n = 3 per group. * P < .05 and ** P < .01
Rabbit Anti Phospho Tak1, supplied by Affinity Biosciences, 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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Average 90 stars, based on 1 article reviews
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Wuhan Sanying Biotechnology antibodies for tak1, ikb-α, p-ikb-α, p65, and p-p65
SHP‐1 negatively regulates kinase phosphorylation in LPS‐treated rMC‐1 cells. A, Effects of SHP‐1 overexpression on inflammatory signalling pathways. Blank‐rLV‐ and SHP‐1‐rLV‐ transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15 or 30 min, and Western blotting was performed to determine the phosphorylation status of <t>TAK1,</t> JNK and NF‐κB and the total protein levels of JNK and NF‐κB. B‐D, Quantitative analysis of pTAK1/β‐actin (B), pJNK/JNK (C) and pNF‐κB/NF‐κB (D). E, Effects of SHP‐1 knockdown on inflammatory signalling pathways. Blank‐rLV‐ and shRNA‐SHP‐1‐rLV‐transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15, or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. F‐H, Quantitative analysis of pTAK1/β‐actin (F), pJNK/JNK (G) and pNF‐κB/NF‐κB (H). Two‐way ANOVA followed by Dunnett's test was used. n = 3 per group. * P < .05 and ** P < .01
Antibodies For Tak1, Ikb α, P Ikb α, P65, And P P65, supplied by Wuhan Sanying Biotechnology, 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 for tak1, ikb-α, p-ikb-α, p65, and p-p65/product/Wuhan Sanying Biotechnology
Average 90 stars, based on 1 article reviews
antibodies for tak1, ikb-α, p-ikb-α, p65, and p-p65 - by Bioz Stars, 2026-03
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GeneTex primary antibodies against tak1 l
SHP‐1 negatively regulates kinase phosphorylation in LPS‐treated rMC‐1 cells. A, Effects of SHP‐1 overexpression on inflammatory signalling pathways. Blank‐rLV‐ and SHP‐1‐rLV‐ transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15 or 30 min, and Western blotting was performed to determine the phosphorylation status of <t>TAK1,</t> JNK and NF‐κB and the total protein levels of JNK and NF‐κB. B‐D, Quantitative analysis of pTAK1/β‐actin (B), pJNK/JNK (C) and pNF‐κB/NF‐κB (D). E, Effects of SHP‐1 knockdown on inflammatory signalling pathways. Blank‐rLV‐ and shRNA‐SHP‐1‐rLV‐transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15, or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. F‐H, Quantitative analysis of pTAK1/β‐actin (F), pJNK/JNK (G) and pNF‐κB/NF‐κB (H). Two‐way ANOVA followed by Dunnett's test was used. n = 3 per group. * P < .05 and ** P < .01
Primary Antibodies Against Tak1 L, supplied by GeneTex, 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 antibodies against tak1 l/product/GeneTex
Average 90 stars, based on 1 article reviews
primary antibodies against tak1 l - by Bioz Stars, 2026-03
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Image Search Results


NLRC5 regulates microglial activation via promoting phosphorylation of IKKα/β. ( A ) Representative Western blot image of p-IKKα/β, IKKα/β, p-IκB and IκB in BV2-shCtrl and BV2-sh Nlrc5 cells treated with LPS (10 ng/mL) for different times. Bars represent the relative fold change of p-IKKα/β to IKKα/β ( B ) and p-IκB to IκB ( C ) (n = 5 for each group). ( D ) Representative Western blot image of p-TAK1 and TAK1 in BV2-shCtrl and BV2-sh Nlrc5 cells treated with LPS. ( E ) Bars represent the relative fold change of p-TAK1 to TAK1 (n = 5 for each group). ( F ) Anti-NLRC5 was used to precipitate IKKα/β from BV2-shCtrl and BV2-sh Nlrc5 cell extracts. P-IKKα/β and IKKα/β were subsequently determined by Western blot analysis. ( G ) Representative Western blot image of p-IKKα/β, IKKα/β, p-IκB and IκB in RAW264.7-shCtrl and RAW264.7-sh Nlrc5 cells treated with LPS. Bars represent the relative fold change of p-IKKα/β to IKKα/β. ( H ) and p-IκB to IκB ( I ) (n = 5 for each group). All data were presented as mean ± SEM (( B ), LPS: F (3, 32) = 11.51, p < 0.001; NLRC5: F (1, 32) = 15.95, p < 0.001; Interaction: F (3, 32) = 3.201, p < 0.05; ( C ), LPS: F (3, 32) = 8.843, p < 0.001; NLRC5: F (1, 32) = 9.209, p < 0.01; Interaction: F (3, 32) = 4.286, p < 0.05; ( E ), LPS: F (3, 32) = 5.683, p < 0.01; NLRC5: F (1, 32) = 0.3470, p = 0.5600; Interaction: F (3, 32) = 0.1702, p = 0.9157; ( H ), LPS: (3, 32) = 78.14, p < 0.001; NLRC5: F (1, 32) = 8.092, p < 0.01; Interaction: F (3, 32) = 6.471, p < 0.01; ( I) , LPS: (3, 32) = 47.36, p < 0.001; NLRC5: F (1, 32) = 6.760, p < 0.05; Interaction: F (3, 32) = 3.143, p < 0.05). A two-way ANOVA was used to determine the statistical significance of the two groups. * p ≤ 0.05, ** p ≤ 0.01, and *** p ≤ 0.001. ns: no significant difference. p-IKKα/β: phosphorylated IKKα/β; p-IκB: phosphorylated IκB; p-TAK1: phosphorylated TAK1.

Journal: International Journal of Molecular Sciences

Article Title: NLRC5 Deficiency Reduces LPS-Induced Microglial Activation via Inhibition of NF-κB Signaling and Ameliorates Mice’s Depressive-like Behavior

doi: 10.3390/ijms241713265

Figure Lengend Snippet: NLRC5 regulates microglial activation via promoting phosphorylation of IKKα/β. ( A ) Representative Western blot image of p-IKKα/β, IKKα/β, p-IκB and IκB in BV2-shCtrl and BV2-sh Nlrc5 cells treated with LPS (10 ng/mL) for different times. Bars represent the relative fold change of p-IKKα/β to IKKα/β ( B ) and p-IκB to IκB ( C ) (n = 5 for each group). ( D ) Representative Western blot image of p-TAK1 and TAK1 in BV2-shCtrl and BV2-sh Nlrc5 cells treated with LPS. ( E ) Bars represent the relative fold change of p-TAK1 to TAK1 (n = 5 for each group). ( F ) Anti-NLRC5 was used to precipitate IKKα/β from BV2-shCtrl and BV2-sh Nlrc5 cell extracts. P-IKKα/β and IKKα/β were subsequently determined by Western blot analysis. ( G ) Representative Western blot image of p-IKKα/β, IKKα/β, p-IκB and IκB in RAW264.7-shCtrl and RAW264.7-sh Nlrc5 cells treated with LPS. Bars represent the relative fold change of p-IKKα/β to IKKα/β. ( H ) and p-IκB to IκB ( I ) (n = 5 for each group). All data were presented as mean ± SEM (( B ), LPS: F (3, 32) = 11.51, p < 0.001; NLRC5: F (1, 32) = 15.95, p < 0.001; Interaction: F (3, 32) = 3.201, p < 0.05; ( C ), LPS: F (3, 32) = 8.843, p < 0.001; NLRC5: F (1, 32) = 9.209, p < 0.01; Interaction: F (3, 32) = 4.286, p < 0.05; ( E ), LPS: F (3, 32) = 5.683, p < 0.01; NLRC5: F (1, 32) = 0.3470, p = 0.5600; Interaction: F (3, 32) = 0.1702, p = 0.9157; ( H ), LPS: (3, 32) = 78.14, p < 0.001; NLRC5: F (1, 32) = 8.092, p < 0.01; Interaction: F (3, 32) = 6.471, p < 0.01; ( I) , LPS: (3, 32) = 47.36, p < 0.001; NLRC5: F (1, 32) = 6.760, p < 0.05; Interaction: F (3, 32) = 3.143, p < 0.05). A two-way ANOVA was used to determine the statistical significance of the two groups. * p ≤ 0.05, ** p ≤ 0.01, and *** p ≤ 0.001. ns: no significant difference. p-IKKα/β: phosphorylated IKKα/β; p-IκB: phosphorylated IκB; p-TAK1: phosphorylated TAK1.

Article Snippet: The corresponding antibodies to the protein of interest for immunoblotting included p-IKKα/β (Cell Signaling Technology, Danvers, MA, USA, 2697, 1:1000 dilution), p-I k B (Cell Signaling Technology, 9246, 1:1000 dilution), IKKα/β (Abcam, Cambridge, MA, USA, ab178870, 1:1000 dilution), I k B (Cell Signaling Technology, 9242, 1:1000 dilution), p65 (BD Bioscience, San Jose, CA, USA, 610868, 1:1000 dilution), NLRC5 (Abcam, ab105411, 1:500 dilution), p-TAK1 (ImmunoWay, Plano, TX, USA, YP1522, 1:500 dilution), TAK1 (ImmunoWay, YT4536, 1:1000 dilution), cleaved-Caspase-1 p20 (Santa Cruz Biotechnology, Santa Cruz, CA, USA, sc1218, 1:1000 dilution), β-actin (Sigma-Aldrich, A5441, 1:5000 dilution), and Histone-3 (Cell Signaling Technology, 4499, 1:2000 dilution).

Techniques: Activation Assay, Phospho-proteomics, Western Blot

SHP‐1 negatively regulates kinase phosphorylation in LPS‐treated rMC‐1 cells. A, Effects of SHP‐1 overexpression on inflammatory signalling pathways. Blank‐rLV‐ and SHP‐1‐rLV‐ transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15 or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. B‐D, Quantitative analysis of pTAK1/β‐actin (B), pJNK/JNK (C) and pNF‐κB/NF‐κB (D). E, Effects of SHP‐1 knockdown on inflammatory signalling pathways. Blank‐rLV‐ and shRNA‐SHP‐1‐rLV‐transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15, or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. F‐H, Quantitative analysis of pTAK1/β‐actin (F), pJNK/JNK (G) and pNF‐κB/NF‐κB (H). Two‐way ANOVA followed by Dunnett's test was used. n = 3 per group. * P < .05 and ** P < .01

Journal: Journal of Cellular and Molecular Medicine

Article Title: SHP‐1 suppresses endotoxin‐induced uveitis by inhibiting the TAK1/JNK pathway

doi: 10.1111/jcmm.15888

Figure Lengend Snippet: SHP‐1 negatively regulates kinase phosphorylation in LPS‐treated rMC‐1 cells. A, Effects of SHP‐1 overexpression on inflammatory signalling pathways. Blank‐rLV‐ and SHP‐1‐rLV‐ transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15 or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. B‐D, Quantitative analysis of pTAK1/β‐actin (B), pJNK/JNK (C) and pNF‐κB/NF‐κB (D). E, Effects of SHP‐1 knockdown on inflammatory signalling pathways. Blank‐rLV‐ and shRNA‐SHP‐1‐rLV‐transfected rMC‐1 cells were exposed to 10 μg/mL LPS for 0, 15, or 30 min, and Western blotting was performed to determine the phosphorylation status of TAK1, JNK and NF‐κB and the total protein levels of JNK and NF‐κB. F‐H, Quantitative analysis of pTAK1/β‐actin (F), pJNK/JNK (G) and pNF‐κB/NF‐κB (H). Two‐way ANOVA followed by Dunnett's test was used. n = 3 per group. * P < .05 and ** P < .01

Article Snippet: The proteins were then transferred to a polyvinylidene difluoride membrane (Millipore), which was then blocked with 5% milk for 1 hour and incubated with diluted primary antibodies at 4°C overnight: rabbit anti‐SHP‐1 (ab32559, diluted 1:1000; Abcam); rabbit anti‐cyclooxygenase‐2 (COX2; ab15191, diluted 1:1000; Abcam); rabbit anti‐IL‐1β (AB1832P, diluted 1:1000; Millipore); rabbit anti‐macrophage inflammatory protein‐1α (MIP‐1α) (80044‐T32, diluted 1:800; Sino Biological); mouse anti‐MCP‐1 (66272‐1‐lg, diluted 1:800; Proteintech); rabbit anti‐NF‐κB p65 (4764S, diluted 1:1000; Cell Signaling Technology); rabbit anti‐NF‐κB phospho‐65 (3033S, diluted 1:1000; Cell Signaling Technology); rabbit anti‐SAPK/JNK (9252T, diluted 1:1000; Cell Signaling Technology); rabbit anti‐phospho‐SAPK/JNK (9251S, diluted 1:1000; Cell Signaling Technology); rabbit anti‐phospho‐TAK1 (AF3019, diluted 1:1000; Affinity Biosciences); and horseradish‐peroxidase (HRP)‐conjugated anti‐β‐actin (5125S, diluted 1:2000; Cell Signaling Technology).

Techniques: Over Expression, Transfection, Western Blot, shRNA