pha  (Vector Laboratories)


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    Structured Review

    Vector Laboratories pha
    Pha, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pha/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pha - by Bioz Stars, 2022-05
    94/100 stars

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    Vector Laboratories biotinylated pha l
    Loss of MGAT4A activity does not affect GlcNAc-β-1,6 branching. A , biosynthetic pathway of tetraantennary branched N -glycans. Binding sites of <t>PHA-L</t> are indicated. B , analysis of PHA-L binding to the Consortium of Functional Glycomics ( CFG ) glycan array v. 5.0 indicates a preference for GlcNAc-β-1,6 branched products. The graph shows the data for 100 μg/ml <t>biotinylated-PHA-L</t> (Vector Laboratories) binding to glycans bearing only β-1,4 branching (β -(1,4) ) and the corresponding β-1,6 glycans (β -(1,6) ). Data are given as fluorescence intensity. C , knockdown of MGAT4A in MCF-7 cells shows no significant change in MGAT4B or MGAT5 mRNA levels by qRT-PCR. The graph shows -fold change mRNA expression compared with NTC. n = 3 biological replicates. Error bars represent the S.D. D , fluorescence microscopy of PHA-L stained MGAT4A-KD and NTC cells. No significant loss of PHA-L binding were observed. Images shown are representative of two biological replicates, five images per replicate.
    Biotinylated Pha L, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated pha l/product/Vector Laboratories
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotinylated pha l - by Bioz Stars, 2022-05
    92/100 stars
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    Loss of MGAT4A activity does not affect GlcNAc-β-1,6 branching. A , biosynthetic pathway of tetraantennary branched N -glycans. Binding sites of PHA-L are indicated. B , analysis of PHA-L binding to the Consortium of Functional Glycomics ( CFG ) glycan array v. 5.0 indicates a preference for GlcNAc-β-1,6 branched products. The graph shows the data for 100 μg/ml biotinylated-PHA-L (Vector Laboratories) binding to glycans bearing only β-1,4 branching (β -(1,4) ) and the corresponding β-1,6 glycans (β -(1,6) ). Data are given as fluorescence intensity. C , knockdown of MGAT4A in MCF-7 cells shows no significant change in MGAT4B or MGAT5 mRNA levels by qRT-PCR. The graph shows -fold change mRNA expression compared with NTC. n = 3 biological replicates. Error bars represent the S.D. D , fluorescence microscopy of PHA-L stained MGAT4A-KD and NTC cells. No significant loss of PHA-L binding were observed. Images shown are representative of two biological replicates, five images per replicate.

    Journal: The Journal of Biological Chemistry

    Article Title: MicroRNA-424 Predicts a Role for β-1,4 Branched Glycosylation in Cell Cycle Progression *

    doi: 10.1074/jbc.M115.672220

    Figure Lengend Snippet: Loss of MGAT4A activity does not affect GlcNAc-β-1,6 branching. A , biosynthetic pathway of tetraantennary branched N -glycans. Binding sites of PHA-L are indicated. B , analysis of PHA-L binding to the Consortium of Functional Glycomics ( CFG ) glycan array v. 5.0 indicates a preference for GlcNAc-β-1,6 branched products. The graph shows the data for 100 μg/ml biotinylated-PHA-L (Vector Laboratories) binding to glycans bearing only β-1,4 branching (β -(1,4) ) and the corresponding β-1,6 glycans (β -(1,6) ). Data are given as fluorescence intensity. C , knockdown of MGAT4A in MCF-7 cells shows no significant change in MGAT4B or MGAT5 mRNA levels by qRT-PCR. The graph shows -fold change mRNA expression compared with NTC. n = 3 biological replicates. Error bars represent the S.D. D , fluorescence microscopy of PHA-L stained MGAT4A-KD and NTC cells. No significant loss of PHA-L binding were observed. Images shown are representative of two biological replicates, five images per replicate.

    Article Snippet: Samples were then blocked with 5% bovine serum albumin in HBSS (2 ml, 30 min) and incubated with primary antibodies or lectins diluted in HBSS as follows for 1 h at room temperature: α-galectin-3 (1:250), α-E-cadherin (1:500), biotinylated-PHA-L (1:500, Vector Laboratories).

    Techniques: Activity Assay, Binding Assay, Functional Assay, Plasmid Preparation, Fluorescence, Quantitative RT-PCR, Expressing, Microscopy, Staining

    Cell surface asialoglycans regulates CRT-mediated PrCR. a , b Treatment with neuraminidase led to the removal of sialic acids from the cell surface of HL60 cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cell surface sialic acids were examined by staining with EBL (a) and MAL (b) by flow cytometry analysis. EBL, Elderberry Bark Lectin; MAL, Maackia Amurensis Lectin II. c , d Examination of cell surface CRT and PHA-L binding sites on cancer cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Recombinant CRT ( c ) and PHA-L ( d ) binding after treatment were measured by flow cytometry. e , f Phagocytosis of cancer cells with neuraminidase treatment. In vitro Phagocytosis assays were performed with HL60, K562, DLD-1, and SW620 cells treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu) as target cells. Mouse bone marrow-derived ( e ) and human peripheral blood monocyte-derived ( f ) macrophages were used for the assay. Phagocytosis was normalized to the maximal response in the experiments. n = 3. * P

    Journal: Nature Communications

    Article Title: Programmed cell removal by calreticulin in tissue homeostasis and cancer

    doi: 10.1038/s41467-018-05211-7

    Figure Lengend Snippet: Cell surface asialoglycans regulates CRT-mediated PrCR. a , b Treatment with neuraminidase led to the removal of sialic acids from the cell surface of HL60 cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cell surface sialic acids were examined by staining with EBL (a) and MAL (b) by flow cytometry analysis. EBL, Elderberry Bark Lectin; MAL, Maackia Amurensis Lectin II. c , d Examination of cell surface CRT and PHA-L binding sites on cancer cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Recombinant CRT ( c ) and PHA-L ( d ) binding after treatment were measured by flow cytometry. e , f Phagocytosis of cancer cells with neuraminidase treatment. In vitro Phagocytosis assays were performed with HL60, K562, DLD-1, and SW620 cells treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu) as target cells. Mouse bone marrow-derived ( e ) and human peripheral blood monocyte-derived ( f ) macrophages were used for the assay. Phagocytosis was normalized to the maximal response in the experiments. n = 3. * P

    Article Snippet: For CRT-binding experiments, cells were incubated with recombinant calreticulin human Fc fusion protein at 40 µg ml−1 or biotin-PHA-L 6 µg ml− 1 (B-1115, Vector laboratory) for 1 h incubated on ice.

    Techniques: Staining, Flow Cytometry, Cytometry, Binding Assay, Recombinant, In Vitro, Derivative Assay

    Identification of CRT-binding ligands on aged and malignant cells. a Screening for CRT-binding glycans with carbohydrate microarray. Purified CRT-IgG-Fc proteins were used to probe a carbohydrate microarray containing a number of different types of glycans, including N-, O- and sulfated-glycans. Anti-IgG-Fc antibody was used for detecting binding of CRT to glycans. Glyco-antigens were used at 0.05 and 0.25 μg μl −1 (left and right bars for each glycan). n = 3. Error bars represent standard deviation. b PHA-L binding to peritoneal neutrophils and macrophages at 0, 4, 6, 8, 24, and 72 h after thioglycollate injection in MRP8-Bcl2 mice. c , d Examination of cell surface CRT-binding sites on neutrophils. Bone marrow ( c ) or peritoneal neutrophils ( d ) were collected and treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cells were incubated with PBS (control; black) or recombinant CRT proteins (red) and binding of CRT was then measured by flow cytometry with PE-conjugated anti-CRT antibody. rCRT binds to mature peritoneal neutrophils but not the immature bone marrow neutrophils. Treatment with neuraminidase led to the release of CRT-binding sites. e , f Immunofluorescent staining of CRT in HL60 ( e ) and SW620 ( f ) cells. CRT localized to perinuclear regions, vesicles, and cell surface. CRT was either expressed at a low level ( e ) or limited to the perinuclear regions ( f ), while a significant portion of PHA-L staining were observed on the cell surface ( e and f ).In a – d , MFI, mean fluorescence intensity

    Journal: Nature Communications

    Article Title: Programmed cell removal by calreticulin in tissue homeostasis and cancer

    doi: 10.1038/s41467-018-05211-7

    Figure Lengend Snippet: Identification of CRT-binding ligands on aged and malignant cells. a Screening for CRT-binding glycans with carbohydrate microarray. Purified CRT-IgG-Fc proteins were used to probe a carbohydrate microarray containing a number of different types of glycans, including N-, O- and sulfated-glycans. Anti-IgG-Fc antibody was used for detecting binding of CRT to glycans. Glyco-antigens were used at 0.05 and 0.25 μg μl −1 (left and right bars for each glycan). n = 3. Error bars represent standard deviation. b PHA-L binding to peritoneal neutrophils and macrophages at 0, 4, 6, 8, 24, and 72 h after thioglycollate injection in MRP8-Bcl2 mice. c , d Examination of cell surface CRT-binding sites on neutrophils. Bone marrow ( c ) or peritoneal neutrophils ( d ) were collected and treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cells were incubated with PBS (control; black) or recombinant CRT proteins (red) and binding of CRT was then measured by flow cytometry with PE-conjugated anti-CRT antibody. rCRT binds to mature peritoneal neutrophils but not the immature bone marrow neutrophils. Treatment with neuraminidase led to the release of CRT-binding sites. e , f Immunofluorescent staining of CRT in HL60 ( e ) and SW620 ( f ) cells. CRT localized to perinuclear regions, vesicles, and cell surface. CRT was either expressed at a low level ( e ) or limited to the perinuclear regions ( f ), while a significant portion of PHA-L staining were observed on the cell surface ( e and f ).In a – d , MFI, mean fluorescence intensity

    Article Snippet: For CRT-binding experiments, cells were incubated with recombinant calreticulin human Fc fusion protein at 40 µg ml−1 or biotin-PHA-L 6 µg ml− 1 (B-1115, Vector laboratory) for 1 h incubated on ice.

    Techniques: Binding Assay, Microarray, Purification, Standard Deviation, Injection, Mouse Assay, Incubation, Recombinant, Flow Cytometry, Cytometry, Staining, Fluorescence

    Cell surface asialoglycans regulates CRT-mediated PrCR. a , b Treatment with neuraminidase led to the removal of sialic acids from the cell surface of HL60 cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cell surface sialic acids were examined by staining with EBL (a) and MAL (b) by flow cytometry analysis. EBL, Elderberry Bark Lectin; MAL, Maackia Amurensis Lectin II. c , d Examination of cell surface CRT and PHA-L binding sites on cancer cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Recombinant CRT ( c ) and PHA-L ( d ) binding after treatment were measured by flow cytometry. e , f Phagocytosis of cancer cells with neuraminidase treatment. In vitro Phagocytosis assays were performed with HL60, K562, DLD-1, and SW620 cells treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu) as target cells. Mouse bone marrow-derived ( e ) and human peripheral blood monocyte-derived ( f ) macrophages were used for the assay. Phagocytosis was normalized to the maximal response in the experiments. n = 3. * P

    Journal: Nature Communications

    Article Title: Programmed cell removal by calreticulin in tissue homeostasis and cancer

    doi: 10.1038/s41467-018-05211-7

    Figure Lengend Snippet: Cell surface asialoglycans regulates CRT-mediated PrCR. a , b Treatment with neuraminidase led to the removal of sialic acids from the cell surface of HL60 cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cell surface sialic acids were examined by staining with EBL (a) and MAL (b) by flow cytometry analysis. EBL, Elderberry Bark Lectin; MAL, Maackia Amurensis Lectin II. c , d Examination of cell surface CRT and PHA-L binding sites on cancer cells. HL60 cells were treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Recombinant CRT ( c ) and PHA-L ( d ) binding after treatment were measured by flow cytometry. e , f Phagocytosis of cancer cells with neuraminidase treatment. In vitro Phagocytosis assays were performed with HL60, K562, DLD-1, and SW620 cells treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu) as target cells. Mouse bone marrow-derived ( e ) and human peripheral blood monocyte-derived ( f ) macrophages were used for the assay. Phagocytosis was normalized to the maximal response in the experiments. n = 3. * P

    Article Snippet: For CRT-binding experiments, cells were incubated with recombinant calreticulin human Fc fusion protein at 40 µg ml−1 or biotin-PHA-L 6 µg ml− 1 (B-1115, Vector laboratory) for 1 h incubated on ice.

    Techniques: Staining, Flow Cytometry, Cytometry, Binding Assay, Recombinant, In Vitro, Derivative Assay

    Identification of CRT-binding ligands on aged and malignant cells. a Screening for CRT-binding glycans with carbohydrate microarray. Purified CRT-IgG-Fc proteins were used to probe a carbohydrate microarray containing a number of different types of glycans, including N-, O- and sulfated-glycans. Anti-IgG-Fc antibody was used for detecting binding of CRT to glycans. Glyco-antigens were used at 0.05 and 0.25 μg μl −1 (left and right bars for each glycan). n = 3. Error bars represent standard deviation. b PHA-L binding to peritoneal neutrophils and macrophages at 0, 4, 6, 8, 24, and 72 h after thioglycollate injection in MRP8-Bcl2 mice. c , d Examination of cell surface CRT-binding sites on neutrophils. Bone marrow ( c ) or peritoneal neutrophils ( d ) were collected and treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cells were incubated with PBS (control; black) or recombinant CRT proteins (red) and binding of CRT was then measured by flow cytometry with PE-conjugated anti-CRT antibody. rCRT binds to mature peritoneal neutrophils but not the immature bone marrow neutrophils. Treatment with neuraminidase led to the release of CRT-binding sites. e , f Immunofluorescent staining of CRT in HL60 ( e ) and SW620 ( f ) cells. CRT localized to perinuclear regions, vesicles, and cell surface. CRT was either expressed at a low level ( e ) or limited to the perinuclear regions ( f ), while a significant portion of PHA-L staining were observed on the cell surface ( e and f ).In a – d , MFI, mean fluorescence intensity

    Journal: Nature Communications

    Article Title: Programmed cell removal by calreticulin in tissue homeostasis and cancer

    doi: 10.1038/s41467-018-05211-7

    Figure Lengend Snippet: Identification of CRT-binding ligands on aged and malignant cells. a Screening for CRT-binding glycans with carbohydrate microarray. Purified CRT-IgG-Fc proteins were used to probe a carbohydrate microarray containing a number of different types of glycans, including N-, O- and sulfated-glycans. Anti-IgG-Fc antibody was used for detecting binding of CRT to glycans. Glyco-antigens were used at 0.05 and 0.25 μg μl −1 (left and right bars for each glycan). n = 3. Error bars represent standard deviation. b PHA-L binding to peritoneal neutrophils and macrophages at 0, 4, 6, 8, 24, and 72 h after thioglycollate injection in MRP8-Bcl2 mice. c , d Examination of cell surface CRT-binding sites on neutrophils. Bone marrow ( c ) or peritoneal neutrophils ( d ) were collected and treated with heat inactivated neuraminidase (Δneu) or neuraminidase (neu). Cells were incubated with PBS (control; black) or recombinant CRT proteins (red) and binding of CRT was then measured by flow cytometry with PE-conjugated anti-CRT antibody. rCRT binds to mature peritoneal neutrophils but not the immature bone marrow neutrophils. Treatment with neuraminidase led to the release of CRT-binding sites. e , f Immunofluorescent staining of CRT in HL60 ( e ) and SW620 ( f ) cells. CRT localized to perinuclear regions, vesicles, and cell surface. CRT was either expressed at a low level ( e ) or limited to the perinuclear regions ( f ), while a significant portion of PHA-L staining were observed on the cell surface ( e and f ).In a – d , MFI, mean fluorescence intensity

    Article Snippet: For CRT-binding experiments, cells were incubated with recombinant calreticulin human Fc fusion protein at 40 µg ml−1 or biotin-PHA-L 6 µg ml− 1 (B-1115, Vector laboratory) for 1 h incubated on ice.

    Techniques: Binding Assay, Microarray, Purification, Standard Deviation, Injection, Mouse Assay, Incubation, Recombinant, Flow Cytometry, Cytometry, Staining, Fluorescence

    Results of lectin blotting and western blotting. (A) Lectin blotting validated Sorafenib induced alteration by the biotinylated MAL-I and biotinylated PHA-L. Anti-β-actin antibody was used to show the protein loading. (B) Downregulation of p-ERK in sorafenib-treated MHCC97L and MHCC97H cells. (C) Downregulation of p-ERK in MHCC97L and MHCC97H cells with U0126 treatment. (D) Diagram of the possible mechanism by which sorafenib treatment reduced the expression of Ets-1. sorafenib treatment decreased the expression of Ets-1 by blocking the Ras/Raf/MAPK signaling pathway in HCC cells. MAL-1, Maackia amurensis lecin I; PHA-L, Phaseolus vulgaris leucoagglutinin; p-, phosphorylated; MEK, mitogen activated protein kinase; ERK, extracellular signal-related kinases; Ets-1, erythroblastosis-26; U0126, 1,4-Diamino-2,3-dicyano-1,4-bis (2-aminophenylthio) butadiene.

    Journal: Oncology Letters

    Article Title: Sorafenib induced alteration of protein glycosylation in hepatocellular carcinoma cells

    doi: 10.3892/ol.2017.6177

    Figure Lengend Snippet: Results of lectin blotting and western blotting. (A) Lectin blotting validated Sorafenib induced alteration by the biotinylated MAL-I and biotinylated PHA-L. Anti-β-actin antibody was used to show the protein loading. (B) Downregulation of p-ERK in sorafenib-treated MHCC97L and MHCC97H cells. (C) Downregulation of p-ERK in MHCC97L and MHCC97H cells with U0126 treatment. (D) Diagram of the possible mechanism by which sorafenib treatment reduced the expression of Ets-1. sorafenib treatment decreased the expression of Ets-1 by blocking the Ras/Raf/MAPK signaling pathway in HCC cells. MAL-1, Maackia amurensis lecin I; PHA-L, Phaseolus vulgaris leucoagglutinin; p-, phosphorylated; MEK, mitogen activated protein kinase; ERK, extracellular signal-related kinases; Ets-1, erythroblastosis-26; U0126, 1,4-Diamino-2,3-dicyano-1,4-bis (2-aminophenylthio) butadiene.

    Article Snippet: Membranes were blocked for nonspecific binding with 3% BSA-TBST at room temperature for 1 h and then incubated with biotinylated Maackia amurensis lectin I (MAL-I; catalog no., B-1315; Vector Laboratories, Inc., Burlingame, CA, USA), biotinylated leucoagglutinin (PHA-L; catalog no., B-1115; Vector Laboratories, Inc.) at a dilution of 1:2,000 or a primary monoclonal mouse anti-human β-actin antibody (cat. no. KC-5A08; KangCheng Bio-tech, Shanghai, China) at a dilution of 1:2,000 at room temperature for 30 min.

    Techniques: Western Blot, Expressing, Blocking Assay