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Rabbit anti tak1

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Rabbit anti-TAK1 is a primary antibody that specifically recognizes the TAK1 (Transforming Growth Factor-Beta Activated Kinase 1) protein. TAK1 is a serine/threonine protein kinase that plays a critical role in various cellular signaling pathways, including the activation of NF-κB and MAPK cascades in response to inflammatory stimuli and stress.

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Lab products found in correlation

Rabbit anti phospho tak1, by Cell Signaling Technology (3 mentions) Rabbit anti iκbα, by Cell Signaling Technology (2 mentions) Bis tris gradient gel, by Thermo Fisher Scientific (2 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (2 mentions) Rabbit anti phospho smad1 5 8, by Cell Signaling Technology (2 mentions) Nupage lds sample loading buffer, by Thermo Fisher Scientific (2 mentions) Rabbit anti smad 1 5 8, by Cell Signaling Technology (2 mentions) Horseradish peroxidase conjugated anti rabbit 1 1000, by GE Healthcare (2 mentions) Supersignal west pico chemiluminescenct substrate kit, by Thermo Fisher Scientific (2 mentions) Mouse anti β actin, by Merck Group (2 mentions) β mercaptoethanol, by Merck Group (2 mentions) Complete mini, by Roche (2 mentions) Rabbit anti β actin, by Cell Signaling Technology (1 mentions) Typhoon fla 9500, by GE Healthcare (1 mentions) Rabbit anti flag, by Cell Signaling Technology (1 mentions) Anti flag m2 antibody, by Merck Group (1 mentions) Anti traf6, by Cell Signaling Technology (1 mentions) Normal rabbit igg, by Merck Group (1 mentions) Anti traf2, by Cell Signaling Technology (1 mentions) Anti tab2, by Cell Signaling Technology (1 mentions)

6 protocols using rabbit anti tak1

1

Western Blot Analysis of Signaling Proteins

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After 48 h transfection, cultured SGC-7901 cells were washed with cold PBS once and lysed with lysis buffer (0.5% NP40). Equal quantities of protein (30 µg) were separated by 10% SDS-PAGE and transferred to nitrocellulose membranes. Membranes were blocked with 5% skimmed milk and incubated with the following primary antibodies, diluted 1:1,000, overnight at 4°C: Rabbit anti-TAK1 (catalog no. 4505), rabbit anti-IκBα (catalog no. 4812), anti-rabbit B-cell lymphoma 2 (Bcl-2; catalog no. 4223), rabbit anti-β-actin (catalog no. 4970) and rabbit anti-Flag (catalog no. 14793), all purchased from Cell Signaling Technology, Inc. Blots were washed with TBS containing Tween 20 (TBST) three times for 10 min each time. Subsequently, membranes were incubated with a horseradish peroxidase-conjugated goat anti-rabbit antibody (1:3,000; catalog no. A00098; GenScript, Piscataway, NJ, USA) for 2 h at room temperature and washed with TBST three times for 10 min each time. Protein bands were visualized using Enhanced Chemiluminescence Plus (Thermo Fisher Scientific, Inc.) and scanned by Typhoon™ FLA 9500 (GE Healthcare Life Sciences, Chalfont, UK). Densitometry was quantified using Image J software (National Institutes of Health, Bethesda, MD, USA) and normalized to β-actin.
Chen Y., Zhou B., Xu L., Fan H., Xie J, & Wang D. (2017). MicroRNA-146a promotes gastric cancer cell apoptosis by targeting transforming growth factor β-activated kinase 1. Molecular Medicine Reports, 16(1), 755-763.
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2

Molecular Interactions in TAK1 Signaling

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Anti-phospho-TAK1 (Thr-187), rabbit anti-TAK1, anti-TRAF2, anti-TRAF6, anti-TAB1, anti-TAB2, anti-phospho-IKKα/β (Ser176/180), anti-phospho-MKK7 (Ser-271/Thr-275), and anti-MKK7 antibodies were purchased from Cell Signaling Technology. Anti-TAB3 antibody was from Abcam. Anti-Myc antibody, normal mouse IgG and normal rabbit IgG were from Millipore. Anti-Flag antibody (M2) was obtained from Sigma. Anti-HA, anti-α-Tubulin, and horseradish peroxidase-conjugated secondary antibodies were from Santa Cruz Biotechnology. Rabbit anti-Vpr antibody was provided by National Institutes of Health (NIH) AIDS Research and Reference Reagent Program. Mouse anti-p24 and anti-TAK1 were generated by immunizing mice with the corresponding full length proteins purified form E. coli BL21 (DE3). 4′, 6-diamidino-2-phenylindole (DAPI) and PMA were purchased from Sigma. Fluorescein-conjugated anti-mouse and anti-rabbit secondary antibodies were purchased from Jackson ImmunoResearch Laboratories. Serine/Threonine phosphatase inhibitor Calyculin A was purchased from Cell Signaling Technology.
Liu R., Lin Y., Jia R., Geng Y., Liang C., Tan J, & Qiao W. (2014). HIV-1 Vpr stimulates NF-κB and AP-1 signaling by activating TAK1. Retrovirology, 11, 45.
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3

Bmp7 Signaling Pathway Activation Assay

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Protein extracts were prepared from E7 BPs treated with Bmp7 for 15 or 30 minutes at room temperature. Tissue was treated with RIPA buffer (SIGMA Aldrich) containing protease (Complete mini; Roche) and phosphatase (SIGMA Aldrich) inhibitor tabletsat 4 °C. Tissue was left on ice for 2 hrs with periodic vortexing. Tissue lysates were subsequently denatured at 85 °C for 5 minutes with NuPAGE LDS sample loading buffer (Invitrogen) and β-mercaptoethanol (SIGMA Aldrich). Proteins were then separated using SDS-PAGE on a 4-12% gradient Bis-Tris gel (Invitrogen) and subsequently transferred to nitrocellulose membranes (Invitrogen) over night at 4 °C. The primary antibodies and dilutions used were as follows: Rabbit anti-Tak1 (1:1000, Cell Signaling), Rabbit anti-phospho-Tak1 (1:1000, Cell Signaling), rabbit anti-Smad 1/5/8 (1:1000, Cell Signaling), rabbit anti-phospho Smad 1/5/8 (1:1000, Cell Signaling), mouse anti-β-Actin (1:5000, Sigma Aldrich). Horseradish peroxidase-conjugated anti-rabbit (1:1000) or anti-mouse (1:5000) IgGs were used as secondary antibodies (GE Healthcare). Specific bands were visualized by chemiluminescence using the SuperSignal® West Pico Chemiluminescenct Substrate kit (Thermo Scientific).
Mann Z.F., Thiede B., Chang W., Shin J.B., May-Simera H.L., Lovett M., Corwin J.T, & Kelley M.W. (2014). A gradient of Bmp7 specifies the tonotopic axis in the developing inner ear. Nature communications, 5, 3839.
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4

Western Blot Analysis of Signaling Proteins

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Western blotting was carried out as previously described [27 (link)]. The primary antibodies used in this study were as follows: rabbit anti-Ki-67, rabbit anti-TRAF6 (Millipore), rabbit anti-TAK1, rabbit anti-phospho-TAK1, rabbit anti-IκBα, mouse anti-phospho-IκBα (Cell Signaling Technology), and mouse anti-β-actin (Boster).
Liu J., Xu J., Li H., Sun C., Yu L., Li Y., Shi C., Zhou X., Bian X., Ping Y., Wen Y., Zhao S., Xu H., Ren L., An T., Wang Q, & Yu S. (2015). miR-146b-5p functions as a tumor suppressor by targeting TRAF6 and predicts the prognosis of human gliomas. Oncotarget, 6(30), 29129-29142.
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5

Bmp7 Signaling Pathway Activation Assay

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Protein extracts were prepared from E7 BPs treated with Bmp7 for 15 or 30 minutes at room temperature. Tissue was treated with RIPA buffer (SIGMA Aldrich) containing protease (Complete mini; Roche) and phosphatase (SIGMA Aldrich) inhibitor tabletsat 4 °C. Tissue was left on ice for 2 hrs with periodic vortexing. Tissue lysates were subsequently denatured at 85 °C for 5 minutes with NuPAGE LDS sample loading buffer (Invitrogen) and β-mercaptoethanol (SIGMA Aldrich). Proteins were then separated using SDS-PAGE on a 4-12% gradient Bis-Tris gel (Invitrogen) and subsequently transferred to nitrocellulose membranes (Invitrogen) over night at 4 °C. The primary antibodies and dilutions used were as follows: Rabbit anti-Tak1 (1:1000, Cell Signaling), Rabbit anti-phospho-Tak1 (1:1000, Cell Signaling), rabbit anti-Smad 1/5/8 (1:1000, Cell Signaling), rabbit anti-phospho Smad 1/5/8 (1:1000, Cell Signaling), mouse anti-β-Actin (1:5000, Sigma Aldrich). Horseradish peroxidase-conjugated anti-rabbit (1:1000) or anti-mouse (1:5000) IgGs were used as secondary antibodies (GE Healthcare). Specific bands were visualized by chemiluminescence using the SuperSignal® West Pico Chemiluminescenct Substrate kit (Thermo Scientific).
Mann Z.F., Thiede B., Chang W., Shin J.B., May-Simera H.L., Lovett M., Corwin J.T, & Kelley M.W. (2014). A gradient of Bmp7 specifies the tonotopic axis in the developing inner ear. Nature communications, 5, 3839.
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6

Analyzing Murine Kidney Protein Expression

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Murine kidney tissues were lysed with ice-cold lysis buffer (Thermo Fisher Scientific) supplemented with complete protease and phosphatase inhibitor cocktail (Thermo Fisher Scientific). After centrifugation at 10000 rpm for 5 min, proteins were boiled in Roti-Load1 Buffer (Carl Roth) at 100ºC for 5 min. Proteins were separated on SDS-polyacrylamide gels and transferred to PVDF membranes. The membranes were incubated overnight at 4°C with the following primary antibodies: rabbit anti-α-smooth muscle actin, rabbit anti-collagen I (diluted 1:1000, Abcam), mouse anti-fibronectin (diluted 1:1000, BD Biosciences), rabbit anti-Tak1, rabbit anti-Smad2, rabbit anti-phosphorylated Smad2 (Ser 465/467 , diluted 1:1000, Cell Signaling),
Feger M., Alesutan I., Castor T., Mia S., Musculus K., Voelkl J, & Lang F. (2015). Inhibitory effect of NH4Cl treatment on renal Tgfß1 signaling following unilateral ureteral obstruction. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 37(3).
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