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mouse anti human c jun  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology mouse anti human c jun
    Mouse Anti Human C Jun, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1172 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+anti+human+c+jun/c-Jun/pmc11334407-70-59-63
    Average 95 stars, based on 1172 article reviews
    mouse anti human c jun - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Polymerase Chain Reaction:

    Article Title: c-Jun N-terminal kinase (JNK1) upregulates XIAP-associated factor 1 (XAF1) through interferon regulatory factor 1 (IRF-1) in gastrointestinal cancer.
    Article Snippet: IFN-a was purchased from ScheringPlough Company (Innishannon, Ireland). .. Goat anti-human XAF1 (C-16), rabbit anti-human JNK1 (C-17) and IRF-1 (C-20), mouse anti-human c-Jun (G-4), p-JNK (G-7) and actin (I-10) and horseradish peroxidase-conjugated anti-goat, anti-rabbit and anti-mouse IgG were purchased from Santa Cruz Abbreviations: AP-1, activator protein-1; cDNA, complementary DNA; ERK, extracellular signal-regulated kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GI, gastrointestinal; IFN, interferon; IRF-1, interferon regulatory factor 1; IRF-E, interferon regulatory factor 1-binding element; JNK, c-Jun N-terminal kinase; PCR, polymerase chain reaction; PMA, phorbol-12myristate-13-acetate; RLU, relative luciferase units; siRNA, small-interfering RNA; TNF, tumor necrosis factor; XAF1, X-linked inhibitor of apoptosis protein-associated factor 1; XIAP, X-linked inhibitor of apoptosis protein. ..

    Luciferase:

    Article Title: c-Jun N-terminal kinase (JNK1) upregulates XIAP-associated factor 1 (XAF1) through interferon regulatory factor 1 (IRF-1) in gastrointestinal cancer.
    Article Snippet: IFN-a was purchased from ScheringPlough Company (Innishannon, Ireland). .. Goat anti-human XAF1 (C-16), rabbit anti-human JNK1 (C-17) and IRF-1 (C-20), mouse anti-human c-Jun (G-4), p-JNK (G-7) and actin (I-10) and horseradish peroxidase-conjugated anti-goat, anti-rabbit and anti-mouse IgG were purchased from Santa Cruz Abbreviations: AP-1, activator protein-1; cDNA, complementary DNA; ERK, extracellular signal-regulated kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GI, gastrointestinal; IFN, interferon; IRF-1, interferon regulatory factor 1; IRF-E, interferon regulatory factor 1-binding element; JNK, c-Jun N-terminal kinase; PCR, polymerase chain reaction; PMA, phorbol-12myristate-13-acetate; RLU, relative luciferase units; siRNA, small-interfering RNA; TNF, tumor necrosis factor; XAF1, X-linked inhibitor of apoptosis protein-associated factor 1; XIAP, X-linked inhibitor of apoptosis protein. ..

    Small Interfering RNA:

    Article Title: c-Jun N-terminal kinase (JNK1) upregulates XIAP-associated factor 1 (XAF1) through interferon regulatory factor 1 (IRF-1) in gastrointestinal cancer.
    Article Snippet: IFN-a was purchased from ScheringPlough Company (Innishannon, Ireland). .. Goat anti-human XAF1 (C-16), rabbit anti-human JNK1 (C-17) and IRF-1 (C-20), mouse anti-human c-Jun (G-4), p-JNK (G-7) and actin (I-10) and horseradish peroxidase-conjugated anti-goat, anti-rabbit and anti-mouse IgG were purchased from Santa Cruz Abbreviations: AP-1, activator protein-1; cDNA, complementary DNA; ERK, extracellular signal-regulated kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GI, gastrointestinal; IFN, interferon; IRF-1, interferon regulatory factor 1; IRF-E, interferon regulatory factor 1-binding element; JNK, c-Jun N-terminal kinase; PCR, polymerase chain reaction; PMA, phorbol-12myristate-13-acetate; RLU, relative luciferase units; siRNA, small-interfering RNA; TNF, tumor necrosis factor; XAF1, X-linked inhibitor of apoptosis protein-associated factor 1; XIAP, X-linked inhibitor of apoptosis protein. ..

    Recombinant:

    Article Title: Areca nut-induced metabolic reprogramming and M2 differentiation promote OPMD malignant transformation
    Article Snippet: The chemiluminescence signal was captured by a Gel DocTM XR + Gel documentation system (Bio-Rad, Hercules, CA). .. The following primary antibodies were used: recombinant anti-human CD163 (ab182422, Abcam, Cambridge, UK), rabbit anti-human VCAM-1 (#13,662, Cell Signaling Technology, Massachusetts), rabbit anti-human p-CREB (GTX61045, Genetex, Irvine, CA), rabbit anti-human CREB (GTX112846, Genetex, Irvine, CA), rabbit anti-human EGFR (phosphor Tyr1086, GTX133599, Genetex, Irvine, CA), rabbit anti-human EGFR (GTX100448, Genetex, Irvine, CA), recombinant anti-human phospho-c-Jun (S63, MAB8930, R&D Systems, MN), mouse anti-human c-Jun (sc-166544, Santa Cruz, Texas), rabbit anti-human N-Cadherin (#4061, Cell Signaling Technology, Massachusetts), rabbit anti-human vimentin (GTX100619, Genetex, Irvine, CA), rabbit anti-human claudin-1 (#4933, Cell Signaling Technology, Massachusetts), rabbit anti-human ZO-1 (GTX108627, Genetex, Irvine, CA), mouse anti-human beta-actin (A5441, Sigma-Aldrich, St. Louis, MO). .. The secondary antibodies used in this study were goat anti-mouse IgG antibody (GTX213111-01, GeneTex, Irvine, CA), goat anti-rabbit IgG antibody (GTX213110-01, GeneTex, Irvine, CA), and rabbit anti-goat IgG antibody (GTX228416-01, GeneTex, Irvine, CA).



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    Characterizing Ecad BioID constructs. TurboID was fused to (A) EC2 domain of Ecad (EC-BioID) and (B) C-terminal of Ecad (C-BioID). Proteomic analysis of both constructs identified ephrin-B1 (EfnB1), coxsackie and adenovirus receptor (CAR), P-cadherin (Pcad), desmocollin-3 (Dsc3), desmoglein-2 (Dsg2), integrin β1 (Intβ1), integrin α2 (Intα2), epithelial cell adhesion molecule (EPCAM), chloride intracellular channel protein (CLIC1), and voltage-dependent anion channel 1 (VDAC1) as proteins that were proximal to Ecad. CLIC1 and VDAC1 are primarily found in nuclei and mitochondria, respectively, and are therefore not shown. Proteins are depicted using deposited Protein Data Bank (PDB) structures or predicted from homology modeling using Modeller. The following PDB IDs were used in generating the images: EfnB1, 6P7Y; CAR, 3J6N; TurboID, 4WF2; GFP, 1GFL; Ecad and Pcad, 3Q2V; Dsc3, 5IRY; Dsg2, 5ERD; Intα2, 3K6S; Intβ1, 3IJE; EPCAM, 4MZV; and membrane, POPE. Images were reconstructed using PyMOL. All cytoplasmic domains are schematic representations. GFP localized to intercellular junction in (C) EC-BioID and (D) C-BioID confirming that Ecad was functional. Fluorescent streptavidin (Sta) staining showed that while BioID <t>biotinylated</t> proteins in the presence (+) of exogenous biotin, low levels of biotinylation was observed in the absence (−) of exogenous biotin. Merged images of GFP and Sta show most of the biotinylation occurs near the junction. (Scale bar, 10 µm.)
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    Image Search Results


    Characterizing Ecad BioID constructs. TurboID was fused to (A) EC2 domain of Ecad (EC-BioID) and (B) C-terminal of Ecad (C-BioID). Proteomic analysis of both constructs identified ephrin-B1 (EfnB1), coxsackie and adenovirus receptor (CAR), P-cadherin (Pcad), desmocollin-3 (Dsc3), desmoglein-2 (Dsg2), integrin β1 (Intβ1), integrin α2 (Intα2), epithelial cell adhesion molecule (EPCAM), chloride intracellular channel protein (CLIC1), and voltage-dependent anion channel 1 (VDAC1) as proteins that were proximal to Ecad. CLIC1 and VDAC1 are primarily found in nuclei and mitochondria, respectively, and are therefore not shown. Proteins are depicted using deposited Protein Data Bank (PDB) structures or predicted from homology modeling using Modeller. The following PDB IDs were used in generating the images: EfnB1, 6P7Y; CAR, 3J6N; TurboID, 4WF2; GFP, 1GFL; Ecad and Pcad, 3Q2V; Dsc3, 5IRY; Dsg2, 5ERD; Intα2, 3K6S; Intβ1, 3IJE; EPCAM, 4MZV; and membrane, POPE. Images were reconstructed using PyMOL. All cytoplasmic domains are schematic representations. GFP localized to intercellular junction in (C) EC-BioID and (D) C-BioID confirming that Ecad was functional. Fluorescent streptavidin (Sta) staining showed that while BioID biotinylated proteins in the presence (+) of exogenous biotin, low levels of biotinylation was observed in the absence (−) of exogenous biotin. Merged images of GFP and Sta show most of the biotinylation occurs near the junction. (Scale bar, 10 µm.)

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Mapping transmembrane binding partners for E-cadherin ectodomains

    doi: 10.1073/pnas.2010209117

    Figure Lengend Snippet: Characterizing Ecad BioID constructs. TurboID was fused to (A) EC2 domain of Ecad (EC-BioID) and (B) C-terminal of Ecad (C-BioID). Proteomic analysis of both constructs identified ephrin-B1 (EfnB1), coxsackie and adenovirus receptor (CAR), P-cadherin (Pcad), desmocollin-3 (Dsc3), desmoglein-2 (Dsg2), integrin β1 (Intβ1), integrin α2 (Intα2), epithelial cell adhesion molecule (EPCAM), chloride intracellular channel protein (CLIC1), and voltage-dependent anion channel 1 (VDAC1) as proteins that were proximal to Ecad. CLIC1 and VDAC1 are primarily found in nuclei and mitochondria, respectively, and are therefore not shown. Proteins are depicted using deposited Protein Data Bank (PDB) structures or predicted from homology modeling using Modeller. The following PDB IDs were used in generating the images: EfnB1, 6P7Y; CAR, 3J6N; TurboID, 4WF2; GFP, 1GFL; Ecad and Pcad, 3Q2V; Dsc3, 5IRY; Dsg2, 5ERD; Intα2, 3K6S; Intβ1, 3IJE; EPCAM, 4MZV; and membrane, POPE. Images were reconstructed using PyMOL. All cytoplasmic domains are schematic representations. GFP localized to intercellular junction in (C) EC-BioID and (D) C-BioID confirming that Ecad was functional. Fluorescent streptavidin (Sta) staining showed that while BioID biotinylated proteins in the presence (+) of exogenous biotin, low levels of biotinylation was observed in the absence (−) of exogenous biotin. Merged images of GFP and Sta show most of the biotinylation occurs near the junction. (Scale bar, 10 µm.)

    Article Snippet: Integrin α2β1 heterodimer with c-Jun and c-Fos (R&D catalog no. 5698-A2) was linked to biotinylated protein G by c-Jun antibody (R&D catalog no. MAB2670).

    Techniques: Construct, Membrane, Functional Assay, Staining

    Single molecule AFM force measurements confirm binding partners for Ecad. (A) Schematic of single molecule AFM force measurement experiment. The AFM tip and substrate were functionalized with PEG linkers, some of which were decorated with streptavidin (Sta). Biotinylated Ecad was directly attached to Sta. (B) Ecad showed Ca2+-dependent homophilic interactions. (C) Biotinylated Dsc3 directly immobilized on Sta (D) showed Ca2+-dependent homophilic interactions and Ca2+-independent heterophilic interactions with Ecad. (E) Intα2β1 heterodimer tagged with c-Jun was immobilized using an anti-c-Jun antibody and biotinylated protein G (Pro-G). (F) Intα2β1 formed Ca2+-dependent homophilic complexes and also formed heterophilic complexes with Ecad. (G) Fc-tagged EfnB1 was attached to Sta using biotinylated Pro-G (H) interacted homophilically and also bound heterophilic to Ecad. (I) Biotinylated Pcad attached to Sta (J) showed Ca2+-dependent homophilic and heterotypic interactions. (K) EPCAM-Fc attached to Sta using biotinylated Pro-G (L) formed Ca2+-independent homophilic dimers. However, EPCAM-Fc did not interact heterophilically with Ecad. (M) CAR-Fc immobilized using biotinylated Pro-G (N) showed low probability of heterophilic interactions with Ecad. Error bars are SE calculated using bootstrap with replacement.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Mapping transmembrane binding partners for E-cadherin ectodomains

    doi: 10.1073/pnas.2010209117

    Figure Lengend Snippet: Single molecule AFM force measurements confirm binding partners for Ecad. (A) Schematic of single molecule AFM force measurement experiment. The AFM tip and substrate were functionalized with PEG linkers, some of which were decorated with streptavidin (Sta). Biotinylated Ecad was directly attached to Sta. (B) Ecad showed Ca2+-dependent homophilic interactions. (C) Biotinylated Dsc3 directly immobilized on Sta (D) showed Ca2+-dependent homophilic interactions and Ca2+-independent heterophilic interactions with Ecad. (E) Intα2β1 heterodimer tagged with c-Jun was immobilized using an anti-c-Jun antibody and biotinylated protein G (Pro-G). (F) Intα2β1 formed Ca2+-dependent homophilic complexes and also formed heterophilic complexes with Ecad. (G) Fc-tagged EfnB1 was attached to Sta using biotinylated Pro-G (H) interacted homophilically and also bound heterophilic to Ecad. (I) Biotinylated Pcad attached to Sta (J) showed Ca2+-dependent homophilic and heterotypic interactions. (K) EPCAM-Fc attached to Sta using biotinylated Pro-G (L) formed Ca2+-independent homophilic dimers. However, EPCAM-Fc did not interact heterophilically with Ecad. (M) CAR-Fc immobilized using biotinylated Pro-G (N) showed low probability of heterophilic interactions with Ecad. Error bars are SE calculated using bootstrap with replacement.

    Article Snippet: Integrin α2β1 heterodimer with c-Jun and c-Fos (R&D catalog no. 5698-A2) was linked to biotinylated protein G by c-Jun antibody (R&D catalog no. MAB2670).

    Techniques: Binding Assay