c18 ziptip Search Results


ziptip c18 tips ztc18s096  (Merck KGaA)
90
Merck KGaA ziptip c18 tips ztc18s096
Ziptip C18 Tips Ztc18s096, supplied by Merck KGaA, 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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ziptip® c4 micro-columns  (Merck KGaA)
90
Merck KGaA ziptip® c4 micro-columns
Ziptip® C4 Micro Columns, supplied by Merck KGaA, 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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c18 zip-tip  (Merck KGaA)
90
Merck KGaA c18 zip-tip
C18 Zip Tip, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c18+ziptip/c18+ziptips/pmc04917241-76-6-8
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desalted peptides ziptip c18  (Merck KGaA)
90
Merck KGaA desalted peptides ziptip c18
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
Desalted Peptides Ziptip C18, supplied by Merck KGaA, 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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ziptip c18 pipette tips ztc18s960  (Merck KGaA)
90
Merck KGaA ziptip c18 pipette tips ztc18s960
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
Ziptip C18 Pipette Tips Ztc18s960, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c18+ziptip/c18+ziptip+ztc18s960/pm27561105-45-5-10
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c18 ziptips  (Eksigent Technologies LLC)
90
Eksigent Technologies LLC c18 ziptips
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
C18 Ziptips, supplied by Eksigent Technologies LLC, 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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Average 90 stars, based on 1 article reviews
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ziptip c18 tips  (Chemie GmbH)
90
Chemie GmbH ziptip c18 tips
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
Ziptip C18 Tips, supplied by Chemie GmbH, 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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c 18 ziptip® material  (METTLER TOLEDO)
90
METTLER TOLEDO c 18 ziptip® material
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
C 18 Ziptip® Material, supplied by METTLER TOLEDO, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c18+ziptip/c+18+ziptip++material/pmc07550026-279-5-9
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c18 ziptip columns  (METTLER TOLEDO)
90
METTLER TOLEDO c18 ziptip columns
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
C18 Ziptip Columns, supplied by METTLER TOLEDO, 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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the ziptip c18 pipette tip for sample purification  (Merck KGaA)
90
Merck KGaA the ziptip c18 pipette tip for sample purification
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
The Ziptip C18 Pipette Tip For Sample Purification, supplied by Merck KGaA, 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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c18 ziptip  (CPI International)
90
CPI International c18 ziptip
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
C18 Ziptip, supplied by CPI International, 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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ziptip c18 microcolumns  (Merck KGaA)
90
Merck KGaA ziptip c18 microcolumns
Determination of cleavage site within C-terminal <t>domain</t> <t>(α</t> CTD). ( A ) The cleaved <t>α</t> <t>CTD</t> was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.
Ziptip C18 Microcolumns, supplied by Merck KGaA, 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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Image Search Results


Determination of cleavage site within C-terminal domain (α CTD). ( A ) The cleaved α CTD was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.

Journal: Viruses

Article Title: The Phage-Encoded N -Acetyltransferase Rac Mediates Inactivation of Pseudomonas aeruginosa Transcription by Cleavage of the RNA Polymerase Alpha Subunit

doi: 10.3390/v12090976

Figure Lengend Snippet: Determination of cleavage site within C-terminal domain (α CTD). ( A ) The cleaved α CTD was purified from phage-infected cells using the C-terminally fused Strep II TM -tag (WSHPQFEK) and subjected to Fourier mass spectrometry (APEX-Qe, Bruker Daltonics). The protein mass (including the tag) was calculated from the spectrum (in green) to be 11,157.87 Da, corresponding to the RpoA fragment indicated in bold in the primary sequence. The bottom figure (in black) represents the theoretical spectrum of this α CTD fragment, with a predicted mass of 11,152.96 Da. The cleavage site is located in the flexible linker sequence connecting the two functional domains. ( B ) Alternative determination of cleavage site within the α CTD domain. The entire RNAP complex was purified from phage-infected cells, separated on SDS-PAGE (left panel) and subjected to MALDI-TOF mass spectrometry (right panel). The relevant m/z range is shown. After ten minutes of infection, we noticed the disappearance of the peak corresponding to the original α subunit (38,835 Da), while a single alternative peak at 26,712 ± 1 Da appeared. This mass allowed us to determine the cleavage site within the flexible linker. ( C ) The different domains of RpoA are shown with the exact position of the cleavage site.

Article Snippet: To determine the mass of the α CTD fragment, desalted peptides (ZipTip C18, Merck Millipore) of this domain were dissolved in 0.1% trifluoroacetic acid (TFA) in 60% acetonitril and subjected to Fourier transform ion cyclotron resonance (FTICR) mass spectrometry on an APEX-Qe, equipped with a 9.4 Tesla magnet (Bruker Daltonics, Bremen, Germany).

Techniques: Purification, Infection, Mass Spectrometry, Sequencing, Functional Assay, SDS Page