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tbp proteintech  (Proteintech)
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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
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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