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antiha tag  (Proteintech)


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    Structured Review

    Proteintech antiha tag
    Antiha Tag, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1684 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+ha/HA+Tag+Antibody/pm42786271-83-54-57
    Average 96 stars, based on 1684 article reviews
    antiha tag - by Bioz Stars, 2026-10
    96/100 stars

    Images

    Related Articles

    Cell-Signaling:

    Article Title: OTUD6A promotes de novo pyrimidine synthesis by deubiquitinating and stabilizing CAD in cervical cancer.
    Article Snippet: Carbamoyl-phosphate synthetase II, aspartate transcarbamylase and dihydroorotase (CAD) is a multifunctional, rate-limiting enzyme involved in de novo pyrimidine synthesis.. Its activity is tightly regulated, primarily through phosphorylation and allosteric mechanisms.. However, the contribution of other post-translational modifications to CAD regulation remains largely unexplored.

    Amplification:

    Article Title: OTUD6A promotes de novo pyrimidine synthesis by deubiquitinating and stabilizing CAD in cervical cancer.
    Article Snippet: Carbamoyl-phosphate synthetase II, aspartate transcarbamylase and dihydroorotase (CAD) is a multifunctional, rate-limiting enzyme involved in de novo pyrimidine synthesis.. Its activity is tightly regulated, primarily through phosphorylation and allosteric mechanisms.. However, the contribution of other post-translational modifications to CAD regulation remains largely unexplored.

    other:

    Article Title: E3 ligase LMO7 enhances temozolomide sensitivity by promoting MGMT degradation in lung cancer
    Article Snippet: The following primary antibodies were used: anti-MGMT (17195-1-AP, Proteintech), anti-HA (51064-2-AP, Proteintech), anti-LMO7 (ab224113, Abcam), anti-FLAG (F3165, Sigma–Aldrich), and anti-ubiquitin (sc-8017, Santa Cruz Biotechnology).

    Article Title: BCR::ABL1 tyrosine kinase inhibitors induce ribosome collisions to activate ZAK-dependent ribotoxic stress and apoptosis in chronic myeloid leukemia.
    Article Snippet: Protein band intensities were measured from individual lanes using ImageJ software, subtracted by background signals, and then normalized to controls.

    Western Blot:

    Article Title: Disruption of spike protein N-glycosylation induces its endoplasmic reticulum retention and attenuates SARS-CoV-2 infectivity.
    Article Snippet: .. The antibodies used for western blot analysis were as follows: anti-FLAG (Proteintech, Cat# 20543-1-AP), anti-HA (Proteintech, Cat# 51064-2-AP), anti-SARS-CoV-2 spike S1 (Sino Biological, Cat# 40591-T62), anti-SARS-CoV-2 spike S2 (Sino Biological, Cat# 40590- MM05), anti-SARS-CoV/SARS-CoV-2 nucleocapsid (Sino Biological, Cat# 40143-R001), anti-His(Beyotime, Cat# AF2870), anti-COPA (Proteintech, Cat# 83089-1-RR), anti-mouse GAPDH (Proteintech, Cat# 60004-1-Ig), anti-GCS1 (Proteintech, Cat# 17859-1-AP), anti-HIV-1 p24 (Proteintech, Cat# 11695), anti-mouse IgG (Sigma-Aldrich, Cat# A5278), and anti-rabbit IgG (Sigma-Aldrich, Cat# A9169). .. The antibodies used for immunofluores cence and flow cytometry were as follows: anti-calnexin (Proteintech, Cat# 10427-2-AP), anti-GM130 (Proteintech, Cat# 11308-1-AP), anti-Lamin B1 (Proteintech, Cat# 12987-1- AP), anti-mouse-FITC (Sigma-Aldrich, Cat# F0257), anti-rabbit-FITC (Sigma-Aldrich, Cat# F9887), anti-human-FITC (Sigma-Aldrich, Cat# F9512), anti-mouse-TRITC (Thermo Fisher Scientific, Cat# A16165), and anti-rabbit-TRITC (Proteintech, Cat# SA00007-2).

    Generated:

    Article Title: Lactylome Reprogramming Mediates Therapeutic Response and Adaptation to Neoadjuvant Chemotherapy in Esophageal Squamous Cell Carcinoma.
    Article Snippet: Anti-GAPDH (PTM-5150), anti-Flag mouse (PTM-6075), anti-pan Kla (PTM-1401RM), Jo urn al Pr -pr oo f Lactylome Profiling Reveals Mechanisms Underlying ESCC Survival Adaptation to Chemotherapy anti-PARP1 (PTM-5171), anti-β-tubulin (PTM-6414), and anti-γ-H2AX (PTM-753) antibodies were purchased from PTM BIO (Hangzhou, China). .. Anti-β-actin (66009-1- Ig), anti-Flag-rabbit (20543-1-AP), anti-HA (51064-2-AP), and anti-SIRT2 (19655-1-AP) antibodies were generated by Proteintech Group (Wuhan, China). .. Anti-pADPr (sc56198) antibody was obtained from Santa Cruz Biotechnology (Dallas, USA).



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    Santa Cruz Biotechnology ha sc7392
    AROS interacts with APC2 of APC/C. (A) Schematic of human APC2. The Cullin homology domain is indicated. APC2 clone C1−41 (amino acids 468-822 of APC2) was isolated in a yeast two-hybrid screen. (B) Interaction of the AROS with APC2 analyzed by yeast two-hybrid assay using LexA DBD-fused AROS in pBTM116 and GAL4 AD-fused APC2 C1−41 in pGAD10. Error bars represent the mean ± standard deviation of three independent experiments. (C) HEK293 cells were lysed, and subjected to IP using <t>anti-IgG</t> or anti-AROS antibody. Western blotting was conducted using the indicated antibodies. (D) HEK293 cells were co-transfected with GFP−AROS and Flag-Empty or Flag–APC2. IP was performed using anti-Flag antibody, and bound proteins were analyzed by Western blotting with anti-GFP antibody. (E) For reverse IP, FLAG–APC2 was co-introduced with Myc–Empty or Myc–AROS into HEK293 cells. IP was performed using anti-Myc antibody, and bound proteins were detected by Western blotting with anti-Flag antibody.
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    Proteintech antiha tag
    AROS interacts with APC2 of APC/C. (A) Schematic of human APC2. The Cullin homology domain is indicated. APC2 clone C1−41 (amino acids 468-822 of APC2) was isolated in a yeast two-hybrid screen. (B) Interaction of the AROS with APC2 analyzed by yeast two-hybrid assay using LexA DBD-fused AROS in pBTM116 and GAL4 AD-fused APC2 C1−41 in pGAD10. Error bars represent the mean ± standard deviation of three independent experiments. (C) HEK293 cells were lysed, and subjected to IP using <t>anti-IgG</t> or anti-AROS antibody. Western blotting was conducted using the indicated antibodies. (D) HEK293 cells were co-transfected with GFP−AROS and Flag-Empty or Flag–APC2. IP was performed using anti-Flag antibody, and bound proteins were analyzed by Western blotting with anti-GFP antibody. (E) For reverse IP, FLAG–APC2 was co-introduced with Myc–Empty or Myc–AROS into HEK293 cells. IP was performed using anti-Myc antibody, and bound proteins were detected by Western blotting with anti-Flag antibody.
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    ABclonal Biotechnology ha antibody
    AROS interacts with APC2 of APC/C. (A) Schematic of human APC2. The Cullin homology domain is indicated. APC2 clone C1−41 (amino acids 468-822 of APC2) was isolated in a yeast two-hybrid screen. (B) Interaction of the AROS with APC2 analyzed by yeast two-hybrid assay using LexA DBD-fused AROS in pBTM116 and GAL4 AD-fused APC2 C1−41 in pGAD10. Error bars represent the mean ± standard deviation of three independent experiments. (C) HEK293 cells were lysed, and subjected to IP using <t>anti-IgG</t> or anti-AROS antibody. Western blotting was conducted using the indicated antibodies. (D) HEK293 cells were co-transfected with GFP−AROS and Flag-Empty or Flag–APC2. IP was performed using anti-Flag antibody, and bound proteins were analyzed by Western blotting with anti-GFP antibody. (E) For reverse IP, FLAG–APC2 was co-introduced with Myc–Empty or Myc–AROS into HEK293 cells. IP was performed using anti-Myc antibody, and bound proteins were detected by Western blotting with anti-Flag antibody.
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    Cell Signaling Technology Inc mouse anti ha
    AROS interacts with APC2 of APC/C. (A) Schematic of human APC2. The Cullin homology domain is indicated. APC2 clone C1−41 (amino acids 468-822 of APC2) was isolated in a yeast two-hybrid screen. (B) Interaction of the AROS with APC2 analyzed by yeast two-hybrid assay using LexA DBD-fused AROS in pBTM116 and GAL4 AD-fused APC2 C1−41 in pGAD10. Error bars represent the mean ± standard deviation of three independent experiments. (C) HEK293 cells were lysed, and subjected to IP using <t>anti-IgG</t> or anti-AROS antibody. Western blotting was conducted using the indicated antibodies. (D) HEK293 cells were co-transfected with GFP−AROS and Flag-Empty or Flag–APC2. IP was performed using anti-Flag antibody, and bound proteins were analyzed by Western blotting with anti-GFP antibody. (E) For reverse IP, FLAG–APC2 was co-introduced with Myc–Empty or Myc–AROS into HEK293 cells. IP was performed using anti-Myc antibody, and bound proteins were detected by Western blotting with anti-Flag antibody.
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    Image Search Results


    AROS interacts with APC2 of APC/C. (A) Schematic of human APC2. The Cullin homology domain is indicated. APC2 clone C1−41 (amino acids 468-822 of APC2) was isolated in a yeast two-hybrid screen. (B) Interaction of the AROS with APC2 analyzed by yeast two-hybrid assay using LexA DBD-fused AROS in pBTM116 and GAL4 AD-fused APC2 C1−41 in pGAD10. Error bars represent the mean ± standard deviation of three independent experiments. (C) HEK293 cells were lysed, and subjected to IP using anti-IgG or anti-AROS antibody. Western blotting was conducted using the indicated antibodies. (D) HEK293 cells were co-transfected with GFP−AROS and Flag-Empty or Flag–APC2. IP was performed using anti-Flag antibody, and bound proteins were analyzed by Western blotting with anti-GFP antibody. (E) For reverse IP, FLAG–APC2 was co-introduced with Myc–Empty or Myc–AROS into HEK293 cells. IP was performed using anti-Myc antibody, and bound proteins were detected by Western blotting with anti-Flag antibody.

    Journal: BMB Reports

    Article Title: APC/C−CDH1 suppresses AROS-mediated protection against DNA damage-induced senescence by ubiquitination

    doi: 10.5483/BMBRep.2025-0031

    Figure Lengend Snippet: AROS interacts with APC2 of APC/C. (A) Schematic of human APC2. The Cullin homology domain is indicated. APC2 clone C1−41 (amino acids 468-822 of APC2) was isolated in a yeast two-hybrid screen. (B) Interaction of the AROS with APC2 analyzed by yeast two-hybrid assay using LexA DBD-fused AROS in pBTM116 and GAL4 AD-fused APC2 C1−41 in pGAD10. Error bars represent the mean ± standard deviation of three independent experiments. (C) HEK293 cells were lysed, and subjected to IP using anti-IgG or anti-AROS antibody. Western blotting was conducted using the indicated antibodies. (D) HEK293 cells were co-transfected with GFP−AROS and Flag-Empty or Flag–APC2. IP was performed using anti-Flag antibody, and bound proteins were analyzed by Western blotting with anti-GFP antibody. (E) For reverse IP, FLAG–APC2 was co-introduced with Myc–Empty or Myc–AROS into HEK293 cells. IP was performed using anti-Myc antibody, and bound proteins were detected by Western blotting with anti-Flag antibody.

    Article Snippet: The following antibodies were used: AROS (sc–86209; Peptron or Santa Cruz Biotechnology), APC2 (12301S, Cell Signaling Technology), CDH1 (ab3242; Abcam), CDC20 (sc13162; Santa Cruz Biotechnology), Cyclin B1 (sc245; Santa Cruz Biotechnology), polyubiquitinated conjugates (BML−PW8805−0500; Enzo Life Science), Flag M2 (F1804; Sigma–Aldrich), Myc (05−724; Merck Millipore), GFP (sc–8334; Santa Cruz Biotechnology), HA (sc7392; Santa Cruz Biotechnology), and β–actin (sc47778; Santa Cruz Biotechnology).

    Techniques: Isolation, Yeast, Two Hybrid Screening, Two Hybrid Assay, Standard Deviation, Western Blot, Transfection

    AROS competes with APC11 for APC2 binding and inhibits APC/C−CDH1-mediated Cyclin B1 degradation. (A, B) AROS competes with APC11 for APC2 binding. (A) In vitro competition assays. GST or GST−APC11 and in vitro -translated Flag–APC2 were used in a GST pull-down assay with increasing amounts of in vitro -translated Myc–AROS. Bound APC2 was detected by Western blotting, using anti-Flag antibody. The decreasing APC2 binding to APC11 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05, **P < 0.01). (B) In vivo competition assays in which HEK293 cells were transfected with GFP−APC11, Flag–APC2, and increasing amounts of Myc–AROS. IP was performed using anti-Flag antibody, and bound APC11 was detected by Western blotting with anti-GFP antibody. The decreasing APC11 binding to APC2 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05). (C, D) AROS suppresses APC/C−CDH1-mediated Cyclin B1 degradation by competing with APC11. (C) Effects of AROS overexpression on APC/C−CDH1-mediated Cyclin Bl degradation. HEK293 cells co-expressing MyC−CDH1 with Flag-AROS were analyzed by Western blotting with the indicated antibodies. The level of Cyclin B1 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05, **P < 0.01). (D) Effect of AROS knockdown on APC/C−CDH1-mediated Cyclin Bl degradation. HEK293 cells were co-transfected with MyC−CDH1 and sh–AROS#1 or sh–AROS#2 (shRNA expression vector). Protein levels were assessed by Western blotting with the indicated antibodies. The level of Cyclin B1 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05).

    Journal: BMB Reports

    Article Title: APC/C−CDH1 suppresses AROS-mediated protection against DNA damage-induced senescence by ubiquitination

    doi: 10.5483/BMBRep.2025-0031

    Figure Lengend Snippet: AROS competes with APC11 for APC2 binding and inhibits APC/C−CDH1-mediated Cyclin B1 degradation. (A, B) AROS competes with APC11 for APC2 binding. (A) In vitro competition assays. GST or GST−APC11 and in vitro -translated Flag–APC2 were used in a GST pull-down assay with increasing amounts of in vitro -translated Myc–AROS. Bound APC2 was detected by Western blotting, using anti-Flag antibody. The decreasing APC2 binding to APC11 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05, **P < 0.01). (B) In vivo competition assays in which HEK293 cells were transfected with GFP−APC11, Flag–APC2, and increasing amounts of Myc–AROS. IP was performed using anti-Flag antibody, and bound APC11 was detected by Western blotting with anti-GFP antibody. The decreasing APC11 binding to APC2 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05). (C, D) AROS suppresses APC/C−CDH1-mediated Cyclin B1 degradation by competing with APC11. (C) Effects of AROS overexpression on APC/C−CDH1-mediated Cyclin Bl degradation. HEK293 cells co-expressing MyC−CDH1 with Flag-AROS were analyzed by Western blotting with the indicated antibodies. The level of Cyclin B1 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05, **P < 0.01). (D) Effect of AROS knockdown on APC/C−CDH1-mediated Cyclin Bl degradation. HEK293 cells were co-transfected with MyC−CDH1 and sh–AROS#1 or sh–AROS#2 (shRNA expression vector). Protein levels were assessed by Western blotting with the indicated antibodies. The level of Cyclin B1 was quantified using ImageJ software. Error bars represent the mean ± SD of three independent experiments (*P < 0.05).

    Article Snippet: The following antibodies were used: AROS (sc–86209; Peptron or Santa Cruz Biotechnology), APC2 (12301S, Cell Signaling Technology), CDH1 (ab3242; Abcam), CDC20 (sc13162; Santa Cruz Biotechnology), Cyclin B1 (sc245; Santa Cruz Biotechnology), polyubiquitinated conjugates (BML−PW8805−0500; Enzo Life Science), Flag M2 (F1804; Sigma–Aldrich), Myc (05−724; Merck Millipore), GFP (sc–8334; Santa Cruz Biotechnology), HA (sc7392; Santa Cruz Biotechnology), and β–actin (sc47778; Santa Cruz Biotechnology).

    Techniques: Binding Assay, In Vitro, GST Pulldown Assay, Western Blot, Software, In Vivo, Transfection, Over Expression, Expressing, Knockdown, shRNA, Plasmid Preparation