esi qtof maxis impact ii Search Results


97
Bruker Corporation esi qtof ms instrument
Purification of TrMgTx. (A) The chromatogram shows the loading of the supernatant of P. pastoris culture (cultured for 72 h, pH 6, induced with 0.5% MeOH) on a Ni 2+ affinity column and elution with imidazole in isocratic mode. Absorbance was measured at 240 nm (indicated with blue line, left axis) and dotted line denotes the concentration of imidazole in elution buffer (right axis). (B) 16% Tricine–SDS-PAGE illustrates the analysis of fractions collected from Ni 2+ affinity chromatography, where lane labels stand for M : low-molecular-weight (LMW) protein marker, S : raw (unpurified) supernatant, FT : flow through, W : wash with washing buffer, E1 : elution with 0.5 M imidazole, and E2 : elution with 1 M imidazole. A band at 6.5 kDa position (blue arrow) in lane E1 and E2 represents partially purified TrMgTx. (C) RP-HPLC chromatogram of TrMgTx. Partially purified TrMgTx in step 1 (A,B) was applied on RP-HPLC C 18 semi-prep column and eluted with a gradient of 10–30% acetonitrile (shown with dotted line, right axis) over 30 min. Absorbance was recorded at 230 nm (left axis). Numbers indicate the peaks collected. (D) 16% Tricine–SDS-PAGE analysis of fractions collected from the RP-HPLC column. Lanes represent M : LMW protein marker, 1–3 : fractions from corresponding peaks as indicated in RP-HPLC chromatogram (panel C ). The band of 6.5 kDa in lane 2 indicated with a black arrow represents purified <t>TrMgTx.</t> <t>(E)</t> <t>ESI-QTOF-MS</t> spectrum shows the average mass (5980.86 Da) of purified TrMgTx.
Esi Qtof Ms Instrument, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/esi+qtof+maxis+impact+ii/maXis+II/pmc08511391-89-7-14
Average 97 stars, based on 1 article reviews
esi qtof ms instrument - by Bioz Stars, 2026-10
97/100 stars
  Buy from Supplier

99
Bruker Corporation maxis impact ii qtof
Purification of TrMgTx. (A) The chromatogram shows the loading of the supernatant of P. pastoris culture (cultured for 72 h, pH 6, induced with 0.5% MeOH) on a Ni 2+ affinity column and elution with imidazole in isocratic mode. Absorbance was measured at 240 nm (indicated with blue line, left axis) and dotted line denotes the concentration of imidazole in elution buffer (right axis). (B) 16% Tricine–SDS-PAGE illustrates the analysis of fractions collected from Ni 2+ affinity chromatography, where lane labels stand for M : low-molecular-weight (LMW) protein marker, S : raw (unpurified) supernatant, FT : flow through, W : wash with washing buffer, E1 : elution with 0.5 M imidazole, and E2 : elution with 1 M imidazole. A band at 6.5 kDa position (blue arrow) in lane E1 and E2 represents partially purified TrMgTx. (C) RP-HPLC chromatogram of TrMgTx. Partially purified TrMgTx in step 1 (A,B) was applied on RP-HPLC C 18 semi-prep column and eluted with a gradient of 10–30% acetonitrile (shown with dotted line, right axis) over 30 min. Absorbance was recorded at 230 nm (left axis). Numbers indicate the peaks collected. (D) 16% Tricine–SDS-PAGE analysis of fractions collected from the RP-HPLC column. Lanes represent M : LMW protein marker, 1–3 : fractions from corresponding peaks as indicated in RP-HPLC chromatogram (panel C ). The band of 6.5 kDa in lane 2 indicated with a black arrow represents purified <t>TrMgTx.</t> <t>(E)</t> <t>ESI-QTOF-MS</t> spectrum shows the average mass (5980.86 Da) of purified TrMgTx.
Maxis Impact Ii Qtof, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/esi+qtof+maxis+impact+ii/impact+II/pmc10782417-34-14-24
Average 99 stars, based on 1 article reviews
maxis impact ii qtof - by Bioz Stars, 2026-10
99/100 stars
  Buy from Supplier

96
Bruker Corporation maxis iitm qtof mass spectrometer
Purification of TrMgTx. (A) The chromatogram shows the loading of the supernatant of P. pastoris culture (cultured for 72 h, pH 6, induced with 0.5% MeOH) on a Ni 2+ affinity column and elution with imidazole in isocratic mode. Absorbance was measured at 240 nm (indicated with blue line, left axis) and dotted line denotes the concentration of imidazole in elution buffer (right axis). (B) 16% Tricine–SDS-PAGE illustrates the analysis of fractions collected from Ni 2+ affinity chromatography, where lane labels stand for M : low-molecular-weight (LMW) protein marker, S : raw (unpurified) supernatant, FT : flow through, W : wash with washing buffer, E1 : elution with 0.5 M imidazole, and E2 : elution with 1 M imidazole. A band at 6.5 kDa position (blue arrow) in lane E1 and E2 represents partially purified TrMgTx. (C) RP-HPLC chromatogram of TrMgTx. Partially purified TrMgTx in step 1 (A,B) was applied on RP-HPLC C 18 semi-prep column and eluted with a gradient of 10–30% acetonitrile (shown with dotted line, right axis) over 30 min. Absorbance was recorded at 230 nm (left axis). Numbers indicate the peaks collected. (D) 16% Tricine–SDS-PAGE analysis of fractions collected from the RP-HPLC column. Lanes represent M : LMW protein marker, 1–3 : fractions from corresponding peaks as indicated in RP-HPLC chromatogram (panel C ). The band of 6.5 kDa in lane 2 indicated with a black arrow represents purified <t>TrMgTx.</t> <t>(E)</t> <t>ESI-QTOF-MS</t> spectrum shows the average mass (5980.86 Da) of purified TrMgTx.
Maxis Iitm Qtof Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/esi+qtof+maxis+impact+ii/Compass+Hystar/pmc08065156-408-13-19
Average 96 stars, based on 1 article reviews
maxis iitm qtof mass spectrometer - by Bioz Stars, 2026-10
96/100 stars
  Buy from Supplier

Image Search Results


Purification of TrMgTx. (A) The chromatogram shows the loading of the supernatant of P. pastoris culture (cultured for 72 h, pH 6, induced with 0.5% MeOH) on a Ni 2+ affinity column and elution with imidazole in isocratic mode. Absorbance was measured at 240 nm (indicated with blue line, left axis) and dotted line denotes the concentration of imidazole in elution buffer (right axis). (B) 16% Tricine–SDS-PAGE illustrates the analysis of fractions collected from Ni 2+ affinity chromatography, where lane labels stand for M : low-molecular-weight (LMW) protein marker, S : raw (unpurified) supernatant, FT : flow through, W : wash with washing buffer, E1 : elution with 0.5 M imidazole, and E2 : elution with 1 M imidazole. A band at 6.5 kDa position (blue arrow) in lane E1 and E2 represents partially purified TrMgTx. (C) RP-HPLC chromatogram of TrMgTx. Partially purified TrMgTx in step 1 (A,B) was applied on RP-HPLC C 18 semi-prep column and eluted with a gradient of 10–30% acetonitrile (shown with dotted line, right axis) over 30 min. Absorbance was recorded at 230 nm (left axis). Numbers indicate the peaks collected. (D) 16% Tricine–SDS-PAGE analysis of fractions collected from the RP-HPLC column. Lanes represent M : LMW protein marker, 1–3 : fractions from corresponding peaks as indicated in RP-HPLC chromatogram (panel C ). The band of 6.5 kDa in lane 2 indicated with a black arrow represents purified TrMgTx. (E) ESI-QTOF-MS spectrum shows the average mass (5980.86 Da) of purified TrMgTx.

Journal: Frontiers in Pharmacology

Article Title: Optimization of Pichia pastoris Expression System for High-Level Production of Margatoxin

doi: 10.3389/fphar.2021.733610

Figure Lengend Snippet: Purification of TrMgTx. (A) The chromatogram shows the loading of the supernatant of P. pastoris culture (cultured for 72 h, pH 6, induced with 0.5% MeOH) on a Ni 2+ affinity column and elution with imidazole in isocratic mode. Absorbance was measured at 240 nm (indicated with blue line, left axis) and dotted line denotes the concentration of imidazole in elution buffer (right axis). (B) 16% Tricine–SDS-PAGE illustrates the analysis of fractions collected from Ni 2+ affinity chromatography, where lane labels stand for M : low-molecular-weight (LMW) protein marker, S : raw (unpurified) supernatant, FT : flow through, W : wash with washing buffer, E1 : elution with 0.5 M imidazole, and E2 : elution with 1 M imidazole. A band at 6.5 kDa position (blue arrow) in lane E1 and E2 represents partially purified TrMgTx. (C) RP-HPLC chromatogram of TrMgTx. Partially purified TrMgTx in step 1 (A,B) was applied on RP-HPLC C 18 semi-prep column and eluted with a gradient of 10–30% acetonitrile (shown with dotted line, right axis) over 30 min. Absorbance was recorded at 230 nm (left axis). Numbers indicate the peaks collected. (D) 16% Tricine–SDS-PAGE analysis of fractions collected from the RP-HPLC column. Lanes represent M : LMW protein marker, 1–3 : fractions from corresponding peaks as indicated in RP-HPLC chromatogram (panel C ). The band of 6.5 kDa in lane 2 indicated with a black arrow represents purified TrMgTx. (E) ESI-QTOF-MS spectrum shows the average mass (5980.86 Da) of purified TrMgTx.

Article Snippet: Mass spectrometric determinations were performed with an ESI-QTOF-MS instrument (maXis II UHR ESI-QTOF MS, Bruker, Bremen, Germany).

Techniques: Purification, Cell Culture, Affinity Column, Concentration Assay, SDS Page, Affinity Chromatography, Molecular Weight, Marker

Removal of tag from TrMgTx. (A) 16% Tricine–SDS-PAGE analysis of the TrMgTx samples incubated overnight at 25°C without ( lane 1 ) and with ( lane 2 ) factor Xa protease (at 1:200 enzyme to peptide ratio); M : low-molecular-weight protein marker. (B) RP-HPLC chromatogram shows the purification of UrMgTx. After separating the His-tag fragments with Ni + beads, the digested sample was loaded on C 18 column and eluted with a gradient of 10–30% acetonitrile over 25 min. The absorbance was measured at 280 nm (left axis), dotted line shows the acetonitrile gradient (right axis). (C) ESI-QTOF-MS spectrum illustrates the average mass (4178.95 Da) of the purified UrMgTx.

Journal: Frontiers in Pharmacology

Article Title: Optimization of Pichia pastoris Expression System for High-Level Production of Margatoxin

doi: 10.3389/fphar.2021.733610

Figure Lengend Snippet: Removal of tag from TrMgTx. (A) 16% Tricine–SDS-PAGE analysis of the TrMgTx samples incubated overnight at 25°C without ( lane 1 ) and with ( lane 2 ) factor Xa protease (at 1:200 enzyme to peptide ratio); M : low-molecular-weight protein marker. (B) RP-HPLC chromatogram shows the purification of UrMgTx. After separating the His-tag fragments with Ni + beads, the digested sample was loaded on C 18 column and eluted with a gradient of 10–30% acetonitrile over 25 min. The absorbance was measured at 280 nm (left axis), dotted line shows the acetonitrile gradient (right axis). (C) ESI-QTOF-MS spectrum illustrates the average mass (4178.95 Da) of the purified UrMgTx.

Article Snippet: Mass spectrometric determinations were performed with an ESI-QTOF-MS instrument (maXis II UHR ESI-QTOF MS, Bruker, Bremen, Germany).

Techniques: SDS Page, Incubation, Molecular Weight, Marker, Purification