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  • 99
    Thermo Fisher nanolc ms ms
    Nanolc Ms Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1053 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanolc ms ms/product/Thermo Fisher
    Average 99 stars, based on 1053 article reviews
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    nanolc ms ms - by Bioz Stars, 2020-05
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    92
    Waters Corporation nanolc ms ms
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Nanolc Ms Ms, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanolc ms ms/product/Waters Corporation
    Average 92 stars, based on 133 article reviews
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    nanolc ms ms - by Bioz Stars, 2020-05
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    92
    Applied Biomics nanolc ms ms
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Nanolc Ms Ms, supplied by Applied Biomics, used in various techniques. Bioz Stars score: 92/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanolc ms ms/product/Applied Biomics
    Average 92 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    nanolc ms ms - by Bioz Stars, 2020-05
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    92
    Waters Corporation mass spectrometry nanolc ms
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Mass Spectrometry Nanolc Ms, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mass spectrometry nanolc ms/product/Waters Corporation
    Average 92 stars, based on 13 article reviews
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    mass spectrometry nanolc ms - by Bioz Stars, 2020-05
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    93
    Thermo Fisher nanolc ms ms system
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Nanolc Ms Ms System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 53 article reviews
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    92
    Thermo Fisher 3000rslc nanolc ms ms system
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    3000rslc Nanolc Ms Ms System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 16 article reviews
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    85
    Thermo Fisher nanolc ms ms ultimate system
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Nanolc Ms Ms Ultimate System, supplied by Thermo Fisher, 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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    90
    SCIEX nanolc ms
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Nanolc Ms, supplied by SCIEX, used in various techniques. Bioz Stars score: 90/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 34 article reviews
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    85
    Thermo Fisher ultimate 3000 nanolc ms ms system
    Deciphering N -glycan structures and positioning on <t>GAP50</t> protein. A , GAP50 glycopeptides were identified using <t>nanoLC-MS/MS.</t> The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).
    Ultimate 3000 Nanolc Ms Ms System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Agilent technologies nanolc ms ms
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 220 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bruker Corporation nanolc ms ms
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 94/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies nanolc ms ms analysis nanolc ms ms analysis
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms Analysis Nanolc Ms Ms Analysis, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation nanolc ms ms analysis nanolc ms ms analysis
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms Analysis Nanolc Ms Ms Analysis, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bruker Corporation nanolc ms system esquire 3000
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms System Esquire 3000, supplied by Bruker Corporation, 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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    93
    Thermo Fisher ab sciex nanolc ms ms
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Ab Sciex Nanolc Ms Ms, supplied by Thermo Fisher, 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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    88
    SCIEX nanolc ms ms system
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms System, supplied by SCIEX, used in various techniques. Bioz Stars score: 88/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    KYA Technologies Corporation nanolc ms ms system
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms System, supplied by KYA Technologies Corporation, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation nanolc ms ms system
    <t>HPLC</t> of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by <t>NanoLC-MS/MS</t> analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.
    Nanolc Ms Ms System, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Deciphering N -glycan structures and positioning on GAP50 protein. A , GAP50 glycopeptides were identified using nanoLC-MS/MS. The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Unusual N-glycan Structures Required for Trafficking Toxoplasma gondii GAP50 to the Inner Membrane Complex Regulate Host Cell Entry Through Parasite Motility *

    doi: 10.1074/mcp.M111.008953

    Figure Lengend Snippet: Deciphering N -glycan structures and positioning on GAP50 protein. A , GAP50 glycopeptides were identified using nanoLC-MS/MS. The MS/MS spectrum from the parent ion m/z = 1150.48 corresponds to the chymotryptic peptide 227 SNVTSRAW 234 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn228. B , The MS/MS spectrum from parent ion at m/z = 1329.03 corresponds to the tryptic peptide 136 NYTSEALR 143 with the N -glycosylation Hex 8 (HexNAc) 2 in position Asn136. C , The MS/MS spectrum from parent ion at m/z = 1414.31 corresponds to the tryptic peptide 77 VAANEHISFIASPGSNFLGGVSSLNDTR 104 with the N -glycosylation Hex 6 (HexNAc) 2 in position Asn101. Symbols were as follows: p , peptide; ■, N-acetylglucosamine; ●, mannose; ●, hexose. (D-G) Chymotryptic digestion of GAP50-HAFLAG profile using nanoLC-MS. D , Extracted ion chromatograms ( m/z 1150.0, 1231.0 for peak 1; 1245.5, 1326.5, 1407.5 for peak 2; 1261.0, 1342.1, 1423.1, for peak 3; ± 0.2 Da) indicated the elution zone of glycopeptides assigned by MS/MS. E , Combined mass spectrum of the glycopeptides containing Asn228 eluting at 17 min (peak 1). F , Combined mass spectrum of the glycopeptides containing Asn136 eluting at 19 min (peak 2). G , Combined mass spectrum of the glycopeptides containing Asn101 eluting at 23 min (peak 3).

    Article Snippet: Five microliters of chymotrypsin GAP50 digest were analyzed by nanoLC-MS using the nanoACQUITY Ultra-Performance-LC system (UPLC, Waters, Milford, MA) coupled to a SYNAPT High Definition Mass Spectrometry quadrupole time-of-flight tandem mass spectrometer (Waters, Milford, MA) equipped with a nano-electrospray source.

    Techniques: Mass Spectrometry

    HPLC of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by NanoLC-MS/MS analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.

    Journal: PLoS ONE

    Article Title: Two Chromogranin A-Derived Peptides Induce Calcium Entry in Human Neutrophils by Calmodulin-Regulated Calcium Independent Phospholipase A2

    doi: 10.1371/journal.pone.0004501

    Figure Lengend Snippet: HPLC of proteins in PMNs secretions induced by CHR and CAT and implication for innate immunity. A, B) Secretion from PMNs (1.10 8 cells) was induced during 30 min stimulation by (A) 20 µM CHR or (B) 20 µM CAT. The secreted proteins > 3 kDa were purified by RP-HPLC on a Macherey Nagel reverse-phase C18 column (4×250 mm; particle size 5 µM and pore size 100 nm). Numbered peaks in the chromatograms indicate protein fractions subjected to proteomic analyses. (C) Proteomic identification by NanoLC-MS/MS analysis of protein fractions involved in innate immunity (protein identification probability > 93%). The numbered HPLC fractions correspond to the peaks of secreted protein in the chromatograms presented in A and B, respectively.

    Article Snippet: The proteins were digested with 40 µL of 12.5 ng/µL of modified porcine trypsin (Promega, Madison, WI, USA) in 25 mM NH4 HCO3 at 37°C for 14 h. The generated peptides were analyzed directly by NanoLC-MS/MS on an Agilent 1100 Series HPLC-Chip/MS system (Agilent Technologies, Palo Alto, USA) coupled to an HCT Ultra ion trap (Bruker Daltonics, Bremen, Germany).

    Techniques: High Performance Liquid Chromatography, Purification, Mass Spectrometry