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recombinant human hrg β-1  (PeproTech)

 
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    PeproTech recombinant human hrg β-1
    Recombinant Human Hrg β 1, supplied by PeproTech, 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/recombinant human hrg β-1/product/PeproTech
    Average 90 stars, based on 1 article reviews
    recombinant human hrg β-1 - by Bioz Stars, 2026-03
    90/100 stars

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    (A) A549 tumor cells were starved for 48 hours and stimulated for 15 minutes with 7 nM p61-Sema3E or 0.2 nM <t>Heregulin-β1</t> ECD <t>(Hrg-β).</t> ErbB2 was immunoprecipitated and analyzed by immunoblotting with anti–phospho-tyrosine (anti-pY) antibodies. The graph shows the average fold change of band intensity ± SD observed in 3 experiments (normalized to controls). (B) As above, serum-starved A549 cells were stimulated for 15 minutes with 7 nM p61 or 1 nM EGF. Then, EGFR or ErbB3 were immunoprecipitated using appropriate antibodies and analyzed with anti–phospho-tyrosine antibodies. (C) In analogy to the above experiments, ErbB2 phosphorylation in response to p61 or Hrg-β was assayed in HeLa carcinoma cells, either control or Plexin D1 depleted (verified by Western blot analysis). The graph shows the average fold change of band intensity ± SD observed in 3 experiments. (D) Plexin D1 (VSV-tagged) and ErbB2, transfected into HEK293 cells, coprecipitate in a specific complex, as revealed by immunoblotting. Analogous results were obtained upon transfection in COS cells (data not shown). The experiment was repeated 3 times with consistent results. (E) COS cells transfected with VSV-tagged Plexin D1 were preincubated with either 200 nM Lapatinib, or 250 nM PHA-665752 (PHA), or vehicle, for 3 hours. Thereafter, cells were treated for 15 minutes with 7 nM p61 or mock stimulated. Plexin D1 was immunoprecipitated and analyzed with anti–phospho-tyrosine antibodies. (F) Serum-starved A549 cancer cells, expressing endogenous Plexin D1 and ErbB2 receptors, were treated with mock or 7 nM p61-Sema3E for 10 minutes. Plexin D1 copurifying with ErbB2 was revealed by immunoblotting.
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    (A) A549 tumor cells were starved for 48 hours and stimulated for 15 minutes with 7 nM p61-Sema3E or 0.2 nM <t>Heregulin-β1</t> ECD <t>(Hrg-β).</t> ErbB2 was immunoprecipitated and analyzed by immunoblotting with anti–phospho-tyrosine (anti-pY) antibodies. The graph shows the average fold change of band intensity ± SD observed in 3 experiments (normalized to controls). (B) As above, serum-starved A549 cells were stimulated for 15 minutes with 7 nM p61 or 1 nM EGF. Then, EGFR or ErbB3 were immunoprecipitated using appropriate antibodies and analyzed with anti–phospho-tyrosine antibodies. (C) In analogy to the above experiments, ErbB2 phosphorylation in response to p61 or Hrg-β was assayed in HeLa carcinoma cells, either control or Plexin D1 depleted (verified by Western blot analysis). The graph shows the average fold change of band intensity ± SD observed in 3 experiments. (D) Plexin D1 (VSV-tagged) and ErbB2, transfected into HEK293 cells, coprecipitate in a specific complex, as revealed by immunoblotting. Analogous results were obtained upon transfection in COS cells (data not shown). The experiment was repeated 3 times with consistent results. (E) COS cells transfected with VSV-tagged Plexin D1 were preincubated with either 200 nM Lapatinib, or 250 nM PHA-665752 (PHA), or vehicle, for 3 hours. Thereafter, cells were treated for 15 minutes with 7 nM p61 or mock stimulated. Plexin D1 was immunoprecipitated and analyzed with anti–phospho-tyrosine antibodies. (F) Serum-starved A549 cancer cells, expressing endogenous Plexin D1 and ErbB2 receptors, were treated with mock or 7 nM p61-Sema3E for 10 minutes. Plexin D1 copurifying with ErbB2 was revealed by immunoblotting.
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    Image Search Results


    (A) A549 tumor cells were starved for 48 hours and stimulated for 15 minutes with 7 nM p61-Sema3E or 0.2 nM Heregulin-β1 ECD (Hrg-β). ErbB2 was immunoprecipitated and analyzed by immunoblotting with anti–phospho-tyrosine (anti-pY) antibodies. The graph shows the average fold change of band intensity ± SD observed in 3 experiments (normalized to controls). (B) As above, serum-starved A549 cells were stimulated for 15 minutes with 7 nM p61 or 1 nM EGF. Then, EGFR or ErbB3 were immunoprecipitated using appropriate antibodies and analyzed with anti–phospho-tyrosine antibodies. (C) In analogy to the above experiments, ErbB2 phosphorylation in response to p61 or Hrg-β was assayed in HeLa carcinoma cells, either control or Plexin D1 depleted (verified by Western blot analysis). The graph shows the average fold change of band intensity ± SD observed in 3 experiments. (D) Plexin D1 (VSV-tagged) and ErbB2, transfected into HEK293 cells, coprecipitate in a specific complex, as revealed by immunoblotting. Analogous results were obtained upon transfection in COS cells (data not shown). The experiment was repeated 3 times with consistent results. (E) COS cells transfected with VSV-tagged Plexin D1 were preincubated with either 200 nM Lapatinib, or 250 nM PHA-665752 (PHA), or vehicle, for 3 hours. Thereafter, cells were treated for 15 minutes with 7 nM p61 or mock stimulated. Plexin D1 was immunoprecipitated and analyzed with anti–phospho-tyrosine antibodies. (F) Serum-starved A549 cancer cells, expressing endogenous Plexin D1 and ErbB2 receptors, were treated with mock or 7 nM p61-Sema3E for 10 minutes. Plexin D1 copurifying with ErbB2 was revealed by immunoblotting.

    Journal: The Journal of Clinical Investigation

    Article Title: Sema3E-Plexin D1 signaling drives human cancer cell invasiveness and metastatic spreading in mice

    doi: 10.1172/JCI42118

    Figure Lengend Snippet: (A) A549 tumor cells were starved for 48 hours and stimulated for 15 minutes with 7 nM p61-Sema3E or 0.2 nM Heregulin-β1 ECD (Hrg-β). ErbB2 was immunoprecipitated and analyzed by immunoblotting with anti–phospho-tyrosine (anti-pY) antibodies. The graph shows the average fold change of band intensity ± SD observed in 3 experiments (normalized to controls). (B) As above, serum-starved A549 cells were stimulated for 15 minutes with 7 nM p61 or 1 nM EGF. Then, EGFR or ErbB3 were immunoprecipitated using appropriate antibodies and analyzed with anti–phospho-tyrosine antibodies. (C) In analogy to the above experiments, ErbB2 phosphorylation in response to p61 or Hrg-β was assayed in HeLa carcinoma cells, either control or Plexin D1 depleted (verified by Western blot analysis). The graph shows the average fold change of band intensity ± SD observed in 3 experiments. (D) Plexin D1 (VSV-tagged) and ErbB2, transfected into HEK293 cells, coprecipitate in a specific complex, as revealed by immunoblotting. Analogous results were obtained upon transfection in COS cells (data not shown). The experiment was repeated 3 times with consistent results. (E) COS cells transfected with VSV-tagged Plexin D1 were preincubated with either 200 nM Lapatinib, or 250 nM PHA-665752 (PHA), or vehicle, for 3 hours. Thereafter, cells were treated for 15 minutes with 7 nM p61 or mock stimulated. Plexin D1 was immunoprecipitated and analyzed with anti–phospho-tyrosine antibodies. (F) Serum-starved A549 cancer cells, expressing endogenous Plexin D1 and ErbB2 receptors, were treated with mock or 7 nM p61-Sema3E for 10 minutes. Plexin D1 copurifying with ErbB2 was revealed by immunoblotting.

    Article Snippet: Recombinant human Heregulin-β1 Extracellular Domain (Hrg-β) and HGF were from R&D Systems.

    Techniques: Immunoprecipitation, Western Blot, Transfection, Expressing