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  • 93
    New England Biolabs β n acetylhexosaminidase
    Adherence of T. vaginalis strain B7RC2 to human vaginal ectocervical cells is inhibited by full-length but not partially digested TvLG. Human vaginal ectocervical cells were preincubated in media alone ( No TvLG ), mock-treated TvLG ( MTvLG ), or TvLG digested with β- N <t>-acetylhexosaminidase</t> and β-galactosidase ( DTvLG ) for 1 h before the addition of labeled parasites as described under “Experimental Procedures.” The average number of parasites per coverslip was calculated, and the number determined in the absence of TvLG ( No TvLG ) was set as 100% adherence. Results presented are the average of three different experiments performed with a total of nine coverslips. Error bars , S.D.
    β N Acetylhexosaminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore β n acetylglucosaminidase
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N Acetylglucosaminidase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore pnp β n acetylglucosaminide
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    Pnp β N Acetylglucosaminide, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore 4mu β n acetylglucosaminide
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    4mu β N Acetylglucosaminide, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Covance β n acetylglucosamine
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N Acetylglucosamine, supplied by Covance, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    ProZyme β n acetylglucosaminidase
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N Acetylglucosaminidase, supplied by ProZyme, used in various techniques. Bioz Stars score: 89/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    ProZyme β n acetylhexosaminidase treated
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N Acetylhexosaminidase Treated, supplied by ProZyme, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Chemical Industry Co Ltd β n
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N, supplied by Chemical Industry Co Ltd, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    ProZyme β n acetylglucosaminidase guh
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N Acetylglucosaminidase Guh, supplied by ProZyme, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore β n acetylhexosaminidase
    Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N <t>-acetylhexosaminidase</t> (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial
    β N Acetylhexosaminidase, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Seikagaku p nitrophenyl β n acetylglucosaminide
    Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N <t>-acetylhexosaminidase</t> (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial
    P Nitrophenyl β N Acetylglucosaminide, supplied by Seikagaku, used in various techniques. Bioz Stars score: 80/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore β n methyl n
    Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N <t>-acetylhexosaminidase</t> (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial
    β N Methyl N, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    ProZyme β n acetylhexosaminidase
    Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N <t>-acetylhexosaminidase</t> (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial
    β N Acetylhexosaminidase, supplied by ProZyme, used in various techniques. Bioz Stars score: 89/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Seikagaku β n acetylhexosaminidase
    Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N <t>-acetylhexosaminidase</t> (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial
    β N Acetylhexosaminidase, supplied by Seikagaku, used in various techniques. Bioz Stars score: 89/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Roche endo β n acetylglucosaminidase h
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
    Endo β N Acetylglucosaminidase H, supplied by Roche, used in various techniques. Bioz Stars score: 90/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore endo β n acetylglucosaminidase h
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
    Endo β N Acetylglucosaminidase H, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore endo β n acetylglucosaminidase f2
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
    Endo β N Acetylglucosaminidase F2, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    DCP Microdevelopments y β n
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
    Y β N, supplied by DCP Microdevelopments, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs endo β n acetylcosaminidase h
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
    Endo β N Acetylcosaminidase H, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    New England Biolabs endo β n acetylglucosaminidase
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
    Endo β N Acetylglucosaminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore endo β n acetylglucosaminidase f3
    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml <t>endo-β-</t> N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p
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    Image Search Results


    Adherence of T. vaginalis strain B7RC2 to human vaginal ectocervical cells is inhibited by full-length but not partially digested TvLG. Human vaginal ectocervical cells were preincubated in media alone ( No TvLG ), mock-treated TvLG ( MTvLG ), or TvLG digested with β- N -acetylhexosaminidase and β-galactosidase ( DTvLG ) for 1 h before the addition of labeled parasites as described under “Experimental Procedures.” The average number of parasites per coverslip was calculated, and the number determined in the absence of TvLG ( No TvLG ) was set as 100% adherence. Results presented are the average of three different experiments performed with a total of nine coverslips. Error bars , S.D.

    Journal: The Journal of Biological Chemistry

    Article Title: Chemical Structure of Trichomonas vaginalis Surface Lipoglycan

    doi: 10.1074/jbc.M111.280578

    Figure Lengend Snippet: Adherence of T. vaginalis strain B7RC2 to human vaginal ectocervical cells is inhibited by full-length but not partially digested TvLG. Human vaginal ectocervical cells were preincubated in media alone ( No TvLG ), mock-treated TvLG ( MTvLG ), or TvLG digested with β- N -acetylhexosaminidase and β-galactosidase ( DTvLG ) for 1 h before the addition of labeled parasites as described under “Experimental Procedures.” The average number of parasites per coverslip was calculated, and the number determined in the absence of TvLG ( No TvLG ) was set as 100% adherence. Results presented are the average of three different experiments performed with a total of nine coverslips. Error bars , S.D.

    Article Snippet: Exoglycosidase Digestion For enzymatic digestion, TvLG was incubated with 0.5 unit of β-galactosidase (bovine testes; Sigma), 15 units of β-N -acetylhexosaminidase (New England Biolabs), or a combination of the two at 37 °C for 24 h in 50 mm sodium citrate, pH 4.5.

    Techniques: Labeling

    The effects of exoglycosidase digestion on TvLG. A , TvLG digested by β-galactosidase and β- N -acetylhexosaminidase (+) and mock-treated TvLG (−) were resolved by SDS-PAGE on a 12.5% acrylamide gel along with prestained molecular weight marker ( M ). The gel was stained with periodate-Schiff reagent to visualize the carbohydrates. B , the monosaccharide composition of digested ( hatched bars ) and mock-treated ( filled bars ) TvLG was determined, and the molar amount of each monosaccharide was calculated and presented as a ratio to rhamnose.

    Journal: The Journal of Biological Chemistry

    Article Title: Chemical Structure of Trichomonas vaginalis Surface Lipoglycan

    doi: 10.1074/jbc.M111.280578

    Figure Lengend Snippet: The effects of exoglycosidase digestion on TvLG. A , TvLG digested by β-galactosidase and β- N -acetylhexosaminidase (+) and mock-treated TvLG (−) were resolved by SDS-PAGE on a 12.5% acrylamide gel along with prestained molecular weight marker ( M ). The gel was stained with periodate-Schiff reagent to visualize the carbohydrates. B , the monosaccharide composition of digested ( hatched bars ) and mock-treated ( filled bars ) TvLG was determined, and the molar amount of each monosaccharide was calculated and presented as a ratio to rhamnose.

    Article Snippet: Exoglycosidase Digestion For enzymatic digestion, TvLG was incubated with 0.5 unit of β-galactosidase (bovine testes; Sigma), 15 units of β-N -acetylhexosaminidase (New England Biolabs), or a combination of the two at 37 °C for 24 h in 50 mm sodium citrate, pH 4.5.

    Techniques: SDS Page, Acrylamide Gel Assay, Molecular Weight, Marker, Staining

    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N -acetylglucosaminidase (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.

    Journal: PLoS ONE

    Article Title: Chemical Characterization of N-Linked Oligosaccharide As the Antigen Epitope Recognized by an Anti-Sperm Auto-Monoclonal Antibody, Ts4

    doi: 10.1371/journal.pone.0133784

    Figure Lengend Snippet: Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N -acetylglucosaminidase (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.

    Article Snippet: On the other hand, the immunoreactivity of Ts4 against TEX101 was completely abrogated by pre-treating with β-N -acetylglucosaminidase from Canavalia ensiformis (Sigma-Aldrich) ( , lane 9 in upper panel). β-N -acetylglucosaminidase is a highly specific exoglycosidase that catalyzes the hydrolysis of terminal non-reducing GlcNAc residues [ ].

    Techniques: Western Blot, Incubation, SDS Page

    Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N -acetylhexosaminidase (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial

    Journal: Journal of Food Science and Technology

    Article Title: Extracellular chitin deacetylase production in solid state fermentation by native soil isolates of Penicillium monoverticillium and Fusarium oxysporum

    doi: 10.1007/s13197-012-0676-1

    Figure Lengend Snippet: Time scale of chitin deacetylase (CDA) production ( a ), endo-chitinase (chitinase) production ( b ) and β- N -acetylhexosaminidase (NHase) production ( c ) by P. monoverticillium CFR 2 and F. oxysporum CFR 8 in solid state fermentation using commercial

    Article Snippet: One unit of endo-chitinase activity was defined as the amount of enzyme which released 1 μmol of GlcNAc under the reaction conditions and enzyme production in SSF was expressed as U/g IDS (Suresh et al. ). β- N -acetylhexosaminidase (EC 3.2.1.52) activity was assayed using ρ-nitrophenyl- N -acetyl-β-D-glucosaminide (Sigma Chemical Co., St. Louis, USA) as the substrate essentially the procedure reported earlier (Suresh et al. ).

    Techniques: Histone Deacetylase Assay

    hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml endo-β- N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p

    Journal: The Journal of Biological Chemistry

    Article Title: Cys-27 Variant of Human δ-Opioid Receptor Modulates Maturation and Cell Surface Delivery of Phe-27 Variant via Heteromerization

    doi: 10.1074/jbc.M111.305656

    Figure Lengend Snippet: hδOR Cys-27 decreases expression of the mature hδOR Phe-27 variant at the cell surface in stably co-transfected HEK293 i cells. A–E , HEK293 i cells constitutively expressing HA-hδOR Phe-27 were induced or not with tetracycline for 24 h to express Myc-hδOR Cys-27 -FLAG. Receptors were purified from cellular lysates by immunoprecipitation with HA ( A ; E , lanes 1–4 ) or FLAG M2 ( C ; E , lanes 5–8 ) antibodies and subjected to deglycosylation with 50 milliunits/ml endo-β- N -acetylglucosaminidase H ( Endo H ; E , lanes 2 and 6 ) or 50 units/ml peptide N -glycosidase F ( PNGaseF ; E , lanes 4 and 8 ) or were left untreated ( E , lanes 1 , 3, 5 , and 7 ). Samples were analyzed by SDS-PAGE and Western blotting ( WB ) using the indicated antibodies. In panel A , a longer exposure is shown for the outlined squared area of lanes 1 and 5 . In panel C , lane 6 , the parental HEK293 i cells expressing only hδOR Cys-27 was used as a control. The blots were analyzed by densitometric scanning, and the mature receptor/precursor ratio for receptor glycoforms containing two N -glycans was calculated. The histograms in panels B and D represent the means ± S.E. of samples corresponding to lanes 1 and 5 in panel A and lanes 5 and 6 in panel C , respectively, from three independent experiments. The data were analyzed with the unpaired t test. Molecular weight markers are indicated on the right or left of the blots . The precursor and mature receptor forms are shown with open and closed symbols , respectively, as indicated. F , cell surface receptors were analyzed by flow cytometry using HA ( black bars ) and cMyc ( gray bars ) antibodies. The values shown are the means ± S.E. of four to five independent experiments performed in duplicate. The GeoMean values were normalized to those obtained from samples treated with 0 or 500 ng/ml tetracycline for hδOR Phe-27 and hδOR Cys-27 , respectively. The data were analyzed by Bonferroni's Multiple Comparison test after repeated measures one-way analysis of variance before normalization. G , the number of [ 3 H]diprenorphine binding sites was determined by one-point binding assays using cellular membranes. The B max values were normalized to those obtained from cells treated with 500 ng/ml tetracycline and are shown as the means ± S.E. of two independent experiments. ns , not significant, * p

    Article Snippet: Deglycosylation of immunoprecipitated receptors was performed using endo-β- N -acetylglucosaminidase H or peptide N -glycosidase F (both from Roche Applied Science) as described ( ).

    Techniques: Expressing, Variant Assay, Stable Transfection, Transfection, Purification, Immunoprecipitation, SDS Page, Western Blot, Molecular Weight, Flow Cytometry, Cytometry, Binding Assay