vva b 1235 2 pna b 1075 5  (Vector Laboratories)


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    Vector Laboratories vva b 1235 2 pna b 1075 5
    Vva B 1235 2 Pna B 1075 5, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    vva  (Vector Laboratories)


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    Vector Laboratories vva
    Vva, supplied by Vector Laboratories, 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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    vva  (Vector Laboratories)


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    Vector Laboratories vva
    GALNT1/Tn translocates to the ER. A , Immunofluorescence of Tn antigen in multiple gastric cancer cells. B , Co-staining Tn antigen <t>(VVA,</t> green) <t>and</t> <t>GM130</t> (red) in the indicated cells. C , Co-staining Tn antigen (VVA, green) and PDI (red) in the indicated cells. D , Colocalization of GALNT1 (green) and GM130 (red) in AGS cells after overexpression of GALNT1 . E , Colocalization of GALNT1 (green) and PDI (red) in AGS cells after overexpression of GALNT1 . Scale bar: 50μm. F , Schematic illustration of the working hypothesis.
    Vva, supplied by Vector Laboratories, 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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    1) Product Images from "GALNT1 Enhances Malignant Phenotype of Gastric Cancer via Modulating CD44 Glycosylation to Activate the Wnt/β-catenin Signaling Pathway"

    Article Title: GALNT1 Enhances Malignant Phenotype of Gastric Cancer via Modulating CD44 Glycosylation to Activate the Wnt/β-catenin Signaling Pathway

    Journal: International Journal of Biological Sciences

    doi: 10.7150/ijbs.73431

    GALNT1/Tn translocates to the ER. A , Immunofluorescence of Tn antigen in multiple gastric cancer cells. B , Co-staining Tn antigen (VVA, green) and GM130 (red) in the indicated cells. C , Co-staining Tn antigen (VVA, green) and PDI (red) in the indicated cells. D , Colocalization of GALNT1 (green) and GM130 (red) in AGS cells after overexpression of GALNT1 . E , Colocalization of GALNT1 (green) and PDI (red) in AGS cells after overexpression of GALNT1 . Scale bar: 50μm. F , Schematic illustration of the working hypothesis.
    Figure Legend Snippet: GALNT1/Tn translocates to the ER. A , Immunofluorescence of Tn antigen in multiple gastric cancer cells. B , Co-staining Tn antigen (VVA, green) and GM130 (red) in the indicated cells. C , Co-staining Tn antigen (VVA, green) and PDI (red) in the indicated cells. D , Colocalization of GALNT1 (green) and GM130 (red) in AGS cells after overexpression of GALNT1 . E , Colocalization of GALNT1 (green) and PDI (red) in AGS cells after overexpression of GALNT1 . Scale bar: 50μm. F , Schematic illustration of the working hypothesis.

    Techniques Used: Immunofluorescence, Staining, Over Expression

    vva  (Vector Laboratories)


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    Vector Laboratories vva
    Vva, supplied by Vector Laboratories, 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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    biotinylated vva lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated vva lectin
    CD44-Tn and STn glycoproteoforms present high cancer specificity. A) Tn and STn antigens are not expressed in the healthy urothelium, are elevated in cancer, and increased in invasive tumors. The STn antigen, defined by affinity for the anti-tag-72 antibody [B72.3+CC49], is not expressed in the healthy urothelium and is elevated in cancer, being significantly overexpressed in muscle invasive bladder cancer (MIBC). The Tn antigen, based on <t>VVA</t> <t>lectin</t> immunoaffinity, is also not expressed in the healthy urothelium and is elevated in a subset of patients, specially at more advanced stages. B) CD44s colocalizes with Tn and STn antigens in MIBC. CD44 was diffusively expressed across the tumor section without a defined pattern. The STn antigen was observed both in superficial and invasive layers and the Tn antigen was found in scattered niches without a defined expression pattern. Immunohistochemistry also showed the co-localization of CD44 with Tn and STn positive areas in CD44s high tumors, exhibiting low amounts of other isoforms (according to RT-PCR, data not shown). The healthy urothelium expressed high amounts of CD44 and the Tn antigen is present in the cytoplasm of upper stratum umbrella cells while the STn antigen was not detected. C) In situ proximity ligation assays (PLA) supports CD44s-STn glycoproteoforms in MIBC and its presence within tumor invasive fronts. In situ proximity ligation assay showed close spatial proximity between CD44 and STn in the same cells, strongly supporting CD44-STn glycoproteoforms in tumors. This phenotype was mostly observed in invasive fronts of CD44s high tumors and was not detected in the healthy urothelium, suggesting cancer-specificity. D) Double staining immunofluorescence supports CD44s-Tn glycoproteoforms in bladder cancer. CD44s high tumors presented niches of cells co-expressing CD44 and Tn antigen, strongly suggesting CD44-Tn glycoproteoforms. This was not observed in the healthy urothelium. E) Glycosylation with Tn and STn antigens provides cancer specificity to CD44. CD44 was abundantly expressed in all studied healthy tissues. STn expression was either absent or low in secretions and cells facing the lumen of the respiratory, gastrointestinal, and colorectal tracts. Immunohistochemistry suggested STn and CD44 co-localization in the stomach, appendix, small intestine, colon, gallbladder, and white blood cells in MALT. PLA did not confirm these hypotheses, suggesting cancer specificity of CD44-STn glycoproteoforms. In healthy tissues, the Tn was restricted to the cytoplasm of goblet cells in the intestinal tract, Leydig cells in testicular tissue, pancreatic acini, hepatocytes, mucinous cells of the gastric epithelium, alveolar macrophages, and gallbladder epithelium. CD44 and Tn antigen co-expression was suggested in pancreatic tissue, testicle, and gallbladder, which was not confirmed by double staining immunofluorescence.
    Biotinylated Vva Lectin, supplied by Vector Laboratories, 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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    1) Product Images from "Glycoproteogenomics characterizes the CD44 splicing code associated with bladder cancer invasion"

    Article Title: Glycoproteogenomics characterizes the CD44 splicing code associated with bladder cancer invasion

    Journal: Theranostics

    doi: 10.7150/thno.67409

    CD44-Tn and STn glycoproteoforms present high cancer specificity. A) Tn and STn antigens are not expressed in the healthy urothelium, are elevated in cancer, and increased in invasive tumors. The STn antigen, defined by affinity for the anti-tag-72 antibody [B72.3+CC49], is not expressed in the healthy urothelium and is elevated in cancer, being significantly overexpressed in muscle invasive bladder cancer (MIBC). The Tn antigen, based on VVA lectin immunoaffinity, is also not expressed in the healthy urothelium and is elevated in a subset of patients, specially at more advanced stages. B) CD44s colocalizes with Tn and STn antigens in MIBC. CD44 was diffusively expressed across the tumor section without a defined pattern. The STn antigen was observed both in superficial and invasive layers and the Tn antigen was found in scattered niches without a defined expression pattern. Immunohistochemistry also showed the co-localization of CD44 with Tn and STn positive areas in CD44s high tumors, exhibiting low amounts of other isoforms (according to RT-PCR, data not shown). The healthy urothelium expressed high amounts of CD44 and the Tn antigen is present in the cytoplasm of upper stratum umbrella cells while the STn antigen was not detected. C) In situ proximity ligation assays (PLA) supports CD44s-STn glycoproteoforms in MIBC and its presence within tumor invasive fronts. In situ proximity ligation assay showed close spatial proximity between CD44 and STn in the same cells, strongly supporting CD44-STn glycoproteoforms in tumors. This phenotype was mostly observed in invasive fronts of CD44s high tumors and was not detected in the healthy urothelium, suggesting cancer-specificity. D) Double staining immunofluorescence supports CD44s-Tn glycoproteoforms in bladder cancer. CD44s high tumors presented niches of cells co-expressing CD44 and Tn antigen, strongly suggesting CD44-Tn glycoproteoforms. This was not observed in the healthy urothelium. E) Glycosylation with Tn and STn antigens provides cancer specificity to CD44. CD44 was abundantly expressed in all studied healthy tissues. STn expression was either absent or low in secretions and cells facing the lumen of the respiratory, gastrointestinal, and colorectal tracts. Immunohistochemistry suggested STn and CD44 co-localization in the stomach, appendix, small intestine, colon, gallbladder, and white blood cells in MALT. PLA did not confirm these hypotheses, suggesting cancer specificity of CD44-STn glycoproteoforms. In healthy tissues, the Tn was restricted to the cytoplasm of goblet cells in the intestinal tract, Leydig cells in testicular tissue, pancreatic acini, hepatocytes, mucinous cells of the gastric epithelium, alveolar macrophages, and gallbladder epithelium. CD44 and Tn antigen co-expression was suggested in pancreatic tissue, testicle, and gallbladder, which was not confirmed by double staining immunofluorescence.
    Figure Legend Snippet: CD44-Tn and STn glycoproteoforms present high cancer specificity. A) Tn and STn antigens are not expressed in the healthy urothelium, are elevated in cancer, and increased in invasive tumors. The STn antigen, defined by affinity for the anti-tag-72 antibody [B72.3+CC49], is not expressed in the healthy urothelium and is elevated in cancer, being significantly overexpressed in muscle invasive bladder cancer (MIBC). The Tn antigen, based on VVA lectin immunoaffinity, is also not expressed in the healthy urothelium and is elevated in a subset of patients, specially at more advanced stages. B) CD44s colocalizes with Tn and STn antigens in MIBC. CD44 was diffusively expressed across the tumor section without a defined pattern. The STn antigen was observed both in superficial and invasive layers and the Tn antigen was found in scattered niches without a defined expression pattern. Immunohistochemistry also showed the co-localization of CD44 with Tn and STn positive areas in CD44s high tumors, exhibiting low amounts of other isoforms (according to RT-PCR, data not shown). The healthy urothelium expressed high amounts of CD44 and the Tn antigen is present in the cytoplasm of upper stratum umbrella cells while the STn antigen was not detected. C) In situ proximity ligation assays (PLA) supports CD44s-STn glycoproteoforms in MIBC and its presence within tumor invasive fronts. In situ proximity ligation assay showed close spatial proximity between CD44 and STn in the same cells, strongly supporting CD44-STn glycoproteoforms in tumors. This phenotype was mostly observed in invasive fronts of CD44s high tumors and was not detected in the healthy urothelium, suggesting cancer-specificity. D) Double staining immunofluorescence supports CD44s-Tn glycoproteoforms in bladder cancer. CD44s high tumors presented niches of cells co-expressing CD44 and Tn antigen, strongly suggesting CD44-Tn glycoproteoforms. This was not observed in the healthy urothelium. E) Glycosylation with Tn and STn antigens provides cancer specificity to CD44. CD44 was abundantly expressed in all studied healthy tissues. STn expression was either absent or low in secretions and cells facing the lumen of the respiratory, gastrointestinal, and colorectal tracts. Immunohistochemistry suggested STn and CD44 co-localization in the stomach, appendix, small intestine, colon, gallbladder, and white blood cells in MALT. PLA did not confirm these hypotheses, suggesting cancer specificity of CD44-STn glycoproteoforms. In healthy tissues, the Tn was restricted to the cytoplasm of goblet cells in the intestinal tract, Leydig cells in testicular tissue, pancreatic acini, hepatocytes, mucinous cells of the gastric epithelium, alveolar macrophages, and gallbladder epithelium. CD44 and Tn antigen co-expression was suggested in pancreatic tissue, testicle, and gallbladder, which was not confirmed by double staining immunofluorescence.

    Techniques Used: Expressing, Immunohistochemistry, Reverse Transcription Polymerase Chain Reaction, In Situ, Ligation, Proximity Ligation Assay, Double Immunofluorescence Staining

    biotinylated vicia villosa agglutinin vva  (Vector Laboratories)


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    Vector Laboratories biotinylated vicia villosa agglutinin vva
    (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface <t>biotinylated,</t> lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by <t>VVA,</t> which recognizes Tn antigen.
    Biotinylated Vicia Villosa Agglutinin Vva, supplied by Vector Laboratories, 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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    1) Product Images from "COSMC Is Overexpressed in Proliferating Infantile Hemangioma and Enhances Endothelial Cell Growth via VEGFR2"

    Article Title: COSMC Is Overexpressed in Proliferating Infantile Hemangioma and Enhances Endothelial Cell Growth via VEGFR2

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0056211

    (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface biotinylated, lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by VVA, which recognizes Tn antigen.
    Figure Legend Snippet: (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface biotinylated, lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by VVA, which recognizes Tn antigen.

    Techniques Used: Quantitative RT-PCR, Western Blot, Over Expression, Expressing, Binding Assay, Transfection

    biotinylated vicia villosa lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated vicia villosa lectin
    Biotinylated Vicia Villosa Lectin, supplied by Vector Laboratories, 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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    biotinylated vva  (Vector Laboratories)


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    Vector Laboratories biotinylated vva
    Biotinylated Vva, supplied by Vector Laboratories, 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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    biotinylated vicia villosa lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated vicia villosa lectin
    Biotinylated Vicia Villosa Lectin, supplied by Vector Laboratories, 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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    biotinylated vicia villosa lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated vicia villosa lectin
    Biotinylated Vicia Villosa Lectin, supplied by Vector Laboratories, 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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    Vector Laboratories vva b 1235 2 pna b 1075 5
    Vva B 1235 2 Pna B 1075 5, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories vva
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    Vector Laboratories biotinylated vva lectin
    CD44-Tn and STn glycoproteoforms present high cancer specificity. A) Tn and STn antigens are not expressed in the healthy urothelium, are elevated in cancer, and increased in invasive tumors. The STn antigen, defined by affinity for the anti-tag-72 antibody [B72.3+CC49], is not expressed in the healthy urothelium and is elevated in cancer, being significantly overexpressed in muscle invasive bladder cancer (MIBC). The Tn antigen, based on <t>VVA</t> <t>lectin</t> immunoaffinity, is also not expressed in the healthy urothelium and is elevated in a subset of patients, specially at more advanced stages. B) CD44s colocalizes with Tn and STn antigens in MIBC. CD44 was diffusively expressed across the tumor section without a defined pattern. The STn antigen was observed both in superficial and invasive layers and the Tn antigen was found in scattered niches without a defined expression pattern. Immunohistochemistry also showed the co-localization of CD44 with Tn and STn positive areas in CD44s high tumors, exhibiting low amounts of other isoforms (according to RT-PCR, data not shown). The healthy urothelium expressed high amounts of CD44 and the Tn antigen is present in the cytoplasm of upper stratum umbrella cells while the STn antigen was not detected. C) In situ proximity ligation assays (PLA) supports CD44s-STn glycoproteoforms in MIBC and its presence within tumor invasive fronts. In situ proximity ligation assay showed close spatial proximity between CD44 and STn in the same cells, strongly supporting CD44-STn glycoproteoforms in tumors. This phenotype was mostly observed in invasive fronts of CD44s high tumors and was not detected in the healthy urothelium, suggesting cancer-specificity. D) Double staining immunofluorescence supports CD44s-Tn glycoproteoforms in bladder cancer. CD44s high tumors presented niches of cells co-expressing CD44 and Tn antigen, strongly suggesting CD44-Tn glycoproteoforms. This was not observed in the healthy urothelium. E) Glycosylation with Tn and STn antigens provides cancer specificity to CD44. CD44 was abundantly expressed in all studied healthy tissues. STn expression was either absent or low in secretions and cells facing the lumen of the respiratory, gastrointestinal, and colorectal tracts. Immunohistochemistry suggested STn and CD44 co-localization in the stomach, appendix, small intestine, colon, gallbladder, and white blood cells in MALT. PLA did not confirm these hypotheses, suggesting cancer specificity of CD44-STn glycoproteoforms. In healthy tissues, the Tn was restricted to the cytoplasm of goblet cells in the intestinal tract, Leydig cells in testicular tissue, pancreatic acini, hepatocytes, mucinous cells of the gastric epithelium, alveolar macrophages, and gallbladder epithelium. CD44 and Tn antigen co-expression was suggested in pancreatic tissue, testicle, and gallbladder, which was not confirmed by double staining immunofluorescence.
    Biotinylated Vva Lectin, supplied by Vector Laboratories, 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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    Vector Laboratories biotinylated vicia villosa agglutinin vva
    (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface <t>biotinylated,</t> lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by <t>VVA,</t> which recognizes Tn antigen.
    Biotinylated Vicia Villosa Agglutinin Vva, supplied by Vector Laboratories, 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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    93
    Vector Laboratories biotinylated vicia villosa lectin
    (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface <t>biotinylated,</t> lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by <t>VVA,</t> which recognizes Tn antigen.
    Biotinylated Vicia Villosa Lectin, supplied by Vector Laboratories, 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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    Vector Laboratories biotinylated vva
    (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface <t>biotinylated,</t> lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by <t>VVA,</t> which recognizes Tn antigen.
    Biotinylated Vva, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated vva/product/Vector Laboratories
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    Image Search Results


    CD44-Tn and STn glycoproteoforms present high cancer specificity. A) Tn and STn antigens are not expressed in the healthy urothelium, are elevated in cancer, and increased in invasive tumors. The STn antigen, defined by affinity for the anti-tag-72 antibody [B72.3+CC49], is not expressed in the healthy urothelium and is elevated in cancer, being significantly overexpressed in muscle invasive bladder cancer (MIBC). The Tn antigen, based on VVA lectin immunoaffinity, is also not expressed in the healthy urothelium and is elevated in a subset of patients, specially at more advanced stages. B) CD44s colocalizes with Tn and STn antigens in MIBC. CD44 was diffusively expressed across the tumor section without a defined pattern. The STn antigen was observed both in superficial and invasive layers and the Tn antigen was found in scattered niches without a defined expression pattern. Immunohistochemistry also showed the co-localization of CD44 with Tn and STn positive areas in CD44s high tumors, exhibiting low amounts of other isoforms (according to RT-PCR, data not shown). The healthy urothelium expressed high amounts of CD44 and the Tn antigen is present in the cytoplasm of upper stratum umbrella cells while the STn antigen was not detected. C) In situ proximity ligation assays (PLA) supports CD44s-STn glycoproteoforms in MIBC and its presence within tumor invasive fronts. In situ proximity ligation assay showed close spatial proximity between CD44 and STn in the same cells, strongly supporting CD44-STn glycoproteoforms in tumors. This phenotype was mostly observed in invasive fronts of CD44s high tumors and was not detected in the healthy urothelium, suggesting cancer-specificity. D) Double staining immunofluorescence supports CD44s-Tn glycoproteoforms in bladder cancer. CD44s high tumors presented niches of cells co-expressing CD44 and Tn antigen, strongly suggesting CD44-Tn glycoproteoforms. This was not observed in the healthy urothelium. E) Glycosylation with Tn and STn antigens provides cancer specificity to CD44. CD44 was abundantly expressed in all studied healthy tissues. STn expression was either absent or low in secretions and cells facing the lumen of the respiratory, gastrointestinal, and colorectal tracts. Immunohistochemistry suggested STn and CD44 co-localization in the stomach, appendix, small intestine, colon, gallbladder, and white blood cells in MALT. PLA did not confirm these hypotheses, suggesting cancer specificity of CD44-STn glycoproteoforms. In healthy tissues, the Tn was restricted to the cytoplasm of goblet cells in the intestinal tract, Leydig cells in testicular tissue, pancreatic acini, hepatocytes, mucinous cells of the gastric epithelium, alveolar macrophages, and gallbladder epithelium. CD44 and Tn antigen co-expression was suggested in pancreatic tissue, testicle, and gallbladder, which was not confirmed by double staining immunofluorescence.

    Journal: Theranostics

    Article Title: Glycoproteogenomics characterizes the CD44 splicing code associated with bladder cancer invasion

    doi: 10.7150/thno.67409

    Figure Lengend Snippet: CD44-Tn and STn glycoproteoforms present high cancer specificity. A) Tn and STn antigens are not expressed in the healthy urothelium, are elevated in cancer, and increased in invasive tumors. The STn antigen, defined by affinity for the anti-tag-72 antibody [B72.3+CC49], is not expressed in the healthy urothelium and is elevated in cancer, being significantly overexpressed in muscle invasive bladder cancer (MIBC). The Tn antigen, based on VVA lectin immunoaffinity, is also not expressed in the healthy urothelium and is elevated in a subset of patients, specially at more advanced stages. B) CD44s colocalizes with Tn and STn antigens in MIBC. CD44 was diffusively expressed across the tumor section without a defined pattern. The STn antigen was observed both in superficial and invasive layers and the Tn antigen was found in scattered niches without a defined expression pattern. Immunohistochemistry also showed the co-localization of CD44 with Tn and STn positive areas in CD44s high tumors, exhibiting low amounts of other isoforms (according to RT-PCR, data not shown). The healthy urothelium expressed high amounts of CD44 and the Tn antigen is present in the cytoplasm of upper stratum umbrella cells while the STn antigen was not detected. C) In situ proximity ligation assays (PLA) supports CD44s-STn glycoproteoforms in MIBC and its presence within tumor invasive fronts. In situ proximity ligation assay showed close spatial proximity between CD44 and STn in the same cells, strongly supporting CD44-STn glycoproteoforms in tumors. This phenotype was mostly observed in invasive fronts of CD44s high tumors and was not detected in the healthy urothelium, suggesting cancer-specificity. D) Double staining immunofluorescence supports CD44s-Tn glycoproteoforms in bladder cancer. CD44s high tumors presented niches of cells co-expressing CD44 and Tn antigen, strongly suggesting CD44-Tn glycoproteoforms. This was not observed in the healthy urothelium. E) Glycosylation with Tn and STn antigens provides cancer specificity to CD44. CD44 was abundantly expressed in all studied healthy tissues. STn expression was either absent or low in secretions and cells facing the lumen of the respiratory, gastrointestinal, and colorectal tracts. Immunohistochemistry suggested STn and CD44 co-localization in the stomach, appendix, small intestine, colon, gallbladder, and white blood cells in MALT. PLA did not confirm these hypotheses, suggesting cancer specificity of CD44-STn glycoproteoforms. In healthy tissues, the Tn was restricted to the cytoplasm of goblet cells in the intestinal tract, Leydig cells in testicular tissue, pancreatic acini, hepatocytes, mucinous cells of the gastric epithelium, alveolar macrophages, and gallbladder epithelium. CD44 and Tn antigen co-expression was suggested in pancreatic tissue, testicle, and gallbladder, which was not confirmed by double staining immunofluorescence.

    Article Snippet: FFPE bladder tumors and healthy tissue sections were screened by immunohistochemistry for CD44 and Tn and STn antigens, as previously described by Peixoto, A et al . . Tn antigen expression was evaluated using the biotinylated VVA lectin (Vector Laboratories, 40 mg/mL, 1 hour at 37 ºC; ) and the detection of STn and CD44 antigens were performed using the anti-tag-72 (B72.3 + CC49; Abcam, 0.5 mg/mL, overnight at 4 ºC; ) and anti-CD44 (1:5000, ab157107, Abcam; ) antibodies, respectively.

    Techniques: Expressing, Immunohistochemistry, Reverse Transcription Polymerase Chain Reaction, In Situ, Ligation, Proximity Ligation Assay, Double Immunofluorescence Staining

    (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface biotinylated, lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by VVA, which recognizes Tn antigen.

    Journal: PLoS ONE

    Article Title: COSMC Is Overexpressed in Proliferating Infantile Hemangioma and Enhances Endothelial Cell Growth via VEGFR2

    doi: 10.1371/journal.pone.0056211

    Figure Lengend Snippet: (A) Proliferating infantile hemangiomas (IHs) (n = 3 patients) express higher levels of COSMC than HUVECs (n = 3 batches). COSMC mRNA levels were analyzed by real-time RT-PCR. * P <0.05. In lower panel, COSMC is overexpressed in HUVECs. (B) Western blots showing COSMC overexpression (left panel) and knockdown (right panel) in HUVECs. β-actin is a loading control. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (C) COSMC overexpression and knockdown in human endothelial cell line EA.hy926. Relative intensity of signals on Western blots was quantified by ImageQuant5.1. (D) COSMC overexpression and knockdown modulate cell surface carbohydrates on HUVECs. Left panel, COSMC overexpression enhances T synthase and T antigen expression in HUVECs. HUVECs were cell surface biotinylated, lysed, pulled down (PD) with PNA, and then blotted with streptavidin-HRP. The arrow indicated that a protein band with molecular mass of 220-kDa has increased PNA binding in COSMC-transfected HUVECs. Cell lysates were Western blotted for detecting T synthase expression and β-actin was used as a loading control. Right panel, COSMC knockdown increased glycoproteins pulled down by VVA, which recognizes Tn antigen.

    Article Snippet: Sections were incubated with an anti-COSMC polyclonal antibody (1∶30, Sigma, St. Louis, MO), biotinylated peanut agglutinin (PNA) (1∶250, Vector Laboratories, Burlingame, CA), or biotinylated Vicia villosa agglutinin (VVA) (1∶500, Vector Laboratories, Burlingame, CA) diluted with 1% bovine serum albumin (BSA)/PBS for 16 h at 4°C.

    Techniques: Quantitative RT-PCR, Western Blot, Over Expression, Expressing, Binding Assay, Transfection