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complete atcc eagle s minimum essential medium 617 jo urn al pr e p roo f 27 emem  (ATCC)
99
ATCC complete atcc eagle s minimum essential medium 617 jo urn al pr e p roo f 27 emem
Complete Atcc Eagle S Minimum Essential Medium 617 Jo Urn Al Pr E P Roo F 27 Emem, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e coli bl21  (Thermo Fisher)
99
Thermo Fisher e coli bl21
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
E Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rapid e coli 2 medium  (Bio-Rad)
94
Bio-Rad rapid e coli 2 medium
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
Rapid E Coli 2 Medium, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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william e medium  (ATCC)
99
ATCC william e medium
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
William E Medium, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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medium  (ATCC)
94
ATCC medium
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
Medium, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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medium - by Bioz Stars, 2026-04
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medium against e faecalis atcc 29212  (ATCC)
99
ATCC medium against e faecalis atcc 29212
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
Medium Against E Faecalis Atcc 29212, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e medium  (Beijing Solarbio Science)
99
Beijing Solarbio Science e medium
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
E Medium, supplied by Beijing Solarbio Science, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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minimum essential medium e mem  (ATCC)
99
ATCC minimum essential medium e mem
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
Minimum Essential Medium E Mem, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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b5 medium  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology b5 medium
( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, <t>E.</t> <t>coli</t> –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.
B5 Medium, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, E. coli –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.

Journal: Science Advances

Article Title: Phosphorylation of shiftless is important for inhibiting the programmed −1 ribosomal frameshift

doi: 10.1126/sciadv.adw7471

Figure Lengend Snippet: ( A ) EMSAs of the indicated SFL and SFL variants with the 55-nt −1 PRF-short RNA. Increasing protein concentrations used in EMSA are indicated on top of the gels. Representative of three independent experiments. ( B ) SDS-PAGE analysis of purified insect cell–expressed SFL, E. coli –expressed SFL, and insect cell–expressed SFL mutants S249A, T250A, T253A, S256A, S249D, T250D, T253D, and S256D. ( C to G ) BLI titrations of SFL mutants binding with −1 PRF-short RNA. Biotinylated −1 PRF-short RNAs were immobilized on SA biosensors for binding with SFL in solutions with a concentration series indicated on the top right. Binding kinetic parameters K D , k on , and k off are shown on top of each graph. Dashed lines are the fitting of the experimental data. Representative of two independent experiments. (C) Mutants S249A and S249D. (D) Mutants T250A and T250D. (E) Mutants T253A and T253D. (F) Mutants S256A and S256D. (G) Nonphosphorylated SFL expressed from E. coli . ( H ) Histogram illustrating the comparison of K D values of WT SFL and that of SFL mutants from the fitting of representative datasets. Error bars represent the fitting-derived K D error. ( I ) Western blot analyses of insect cell–expressed SFL alone, SFL treated with ALP of different enzyme units (2.5 and 5.0 U), and E. coli –expressed SFL; the samples were stained with SFL pAb or pan phosphor-Ser/Thr mAb. Representative of two independent experiments.

Article Snippet: E. coli BL21 (DE3; Thermo Fisher Scientific, EC0114) cells were grown in Luria-Bertani (LB) medium.

Techniques: SDS Page, Purification, Binding Assay, Concentration Assay, Comparison, Derivative Assay, Western Blot, Staining