cellular protein extractions Search Results


yeast total cellular protein extracts  (Kamada)
90
Kamada yeast total cellular protein extracts
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Yeast Total Cellular Protein Extracts, supplied by Kamada, 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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cellular protein extraction  (PTM Biolabs)
90
PTM Biolabs cellular protein extraction
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Cellular Protein Extraction, supplied by PTM Biolabs, 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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cellular protein extraction - by Bioz Stars, 2026-04
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total cellular protein extraction reagent  (Keygen Biotech)
90
Keygen Biotech total cellular protein extraction reagent
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Total Cellular Protein Extraction Reagent, supplied by Keygen Biotech, 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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total cellular protein extraction kit  (Active Motif)
90
Active Motif total cellular protein extraction kit
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Total Cellular Protein Extraction Kit, supplied by Active Motif, 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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cellular nuclear and cytoplasmic protein extract  (Beyotime)
90
Beyotime cellular nuclear and cytoplasmic protein extract
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Cellular Nuclear And Cytoplasmic Protein Extract, supplied by Beyotime, 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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cellular nuclear and cytoplasmic protein extract - by Bioz Stars, 2026-04
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cellular protein extract  (ICN Biomedicals)
90
ICN Biomedicals cellular protein extract
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Cellular Protein Extract, supplied by ICN Biomedicals, 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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cellular protein extract - by Bioz Stars, 2026-04
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whole cellular proteins extraction and cytosolic fractions preparation procedure  (Beyotime)
90
Beyotime whole cellular proteins extraction and cytosolic fractions preparation procedure
Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote <t>yeast</t> mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total <t>cellular</t> <t>protein</t> <t>extracts</t> were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909
Whole Cellular Proteins Extraction And Cytosolic Fractions Preparation Procedure, supplied by Beyotime, 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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whole cellular proteins extraction and cytosolic fractions preparation procedure - by Bioz Stars, 2026-04
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whole cellular soluble protein fraction extracts (wcf)  (Bruker Corporation)
90
Bruker Corporation whole cellular soluble protein fraction extracts (wcf)
Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in <t>whole</t> <t>cellular</t> fractions <t>(WCF)</t> (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.
Whole Cellular Soluble Protein Fraction Extracts (Wcf), supplied by Bruker Corporation, 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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cellular protein extraction kit  (Beijing Solarbio Science)
90
Beijing Solarbio Science cellular protein extraction kit
Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in <t>whole</t> <t>cellular</t> fractions <t>(WCF)</t> (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.
Cellular Protein Extraction Kit, supplied by Beijing Solarbio Science, 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/result/cellular protein extraction kit/product/Beijing Solarbio Science
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cellular protein extraction kit - by Bioz Stars, 2026-04
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cellular protein extracts  (Upstate Biotechnology Inc)
90
Upstate Biotechnology Inc cellular protein extracts
Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in <t>whole</t> <t>cellular</t> fractions <t>(WCF)</t> (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.
Cellular Protein Extracts, supplied by Upstate Biotechnology Inc, 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/result/cellular protein extracts/product/Upstate Biotechnology Inc
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total cellular protein extracts  (Epizyme Inc)
90
Epizyme Inc total cellular protein extracts
Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in <t>whole</t> <t>cellular</t> fractions <t>(WCF)</t> (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.
Total Cellular Protein Extracts, supplied by Epizyme Inc, 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/result/total cellular protein extracts/product/Epizyme Inc
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cellular protein extraction reagent a supplemented with phenylmethylsulfonyl fluoride (pmsf)  (Beyotime)
90
Beyotime cellular protein extraction reagent a supplemented with phenylmethylsulfonyl fluoride (pmsf)
Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in <t>whole</t> <t>cellular</t> fractions <t>(WCF)</t> (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.
Cellular Protein Extraction Reagent A Supplemented With Phenylmethylsulfonyl Fluoride (Pmsf), supplied by Beyotime, 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


Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote yeast mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total cellular protein extracts were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909

Journal: Yeast (Chichester, England)

Article Title: Yeast Ste23p shares functional similarities with mammalian insulin-degrading enzymes

doi: 10.1002/yea.1709

Figure Lengend Snippet: Characterization of the translation start site of Ste23p. (A) Schematic of the genomic DNA sequence that is 5′ to the predicted start codon of the STE23 open reading frame within pWS482. Schematic is not drawn to scale. (B) The predicted 5′ UTR of STE23 is not required for expression of functional Ste23p. A set of plasmids bearing deletions of the 5′ UTR contained within pWS482 (pWS759-763) and a plasmid lacking part of the STE23 ORF itself (pWS765) were evaluated for their ability to promote yeast mating (top panel) and Ste23p expression (middle panel). Yeast mating was evaluated by mixing MATα cells (IH1793) and M16A-deficient MATa cells (Y272) carrying the indicated plasmid, followed by selection on diploid-selective media. Ste23p expression was evaluated by immunoblotting. Equivalent percentage amounts (2%) of total cellular protein extracts were separated by SDS-PAGE and transferred onto blots that were probed with anti-HA and anti-Act1p antibodies as a loading control (middle and bottom panels, respectively). (C) Expression of Ste23p partially rescues the mating defect of an M16A-deficient yeast strain (Y272). Yeast mating assays and analysis of Ste23p expression were performed as described in (B); the panel order is preserved. WT (IH1783) was transformed with an empty vector (pRS316), and Y272 was transformed with either pRS316 or a plasmid encoding Ste23p-2HA (pWS482). (D) The annotated start codon of STE23 is not required for expression of functional Ste23p. Yeast mating assays and analysis of Ste23p expression were performed as described in (B), using plasmid-transformed Y272 cells, except that 4% of each extract was evaluated; the panel order is preserved. Plasmids used were pWS908-909

Article Snippet: Yeast total cellular protein extracts were prepared as previously described ( Fujimura-Kamada et al. , 1997 ).

Techniques: Sequencing, Expressing, Functional Assay, Plasmid Preparation, Selection, Western Blot, SDS Page, Control, Transformation Assay

Ste23p is expressed in both haploid and diploid yeast. Plasmid-based expression of Ste23p (A) and Axl1p (B) was examined in MATa (IH1783), MATα (IH1784) and diploid (IH1788) cell types, using pWS482 and pWS371, respectively. The steady-state levels of the indicated HA-tagged protein (top panel) and yeast actin (bottom panel) were detected by immunoblotting as described in Figure 6, except that 60% of the total cellular extract preparation was evaluated in the instance of Axl1p samples, due to its low abundance

Journal: Yeast (Chichester, England)

Article Title: Yeast Ste23p shares functional similarities with mammalian insulin-degrading enzymes

doi: 10.1002/yea.1709

Figure Lengend Snippet: Ste23p is expressed in both haploid and diploid yeast. Plasmid-based expression of Ste23p (A) and Axl1p (B) was examined in MATa (IH1783), MATα (IH1784) and diploid (IH1788) cell types, using pWS482 and pWS371, respectively. The steady-state levels of the indicated HA-tagged protein (top panel) and yeast actin (bottom panel) were detected by immunoblotting as described in Figure 6, except that 60% of the total cellular extract preparation was evaluated in the instance of Axl1p samples, due to its low abundance

Article Snippet: Yeast total cellular protein extracts were prepared as previously described ( Fujimura-Kamada et al. , 1997 ).

Techniques: Plasmid Preparation, Expressing, Western Blot

Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in whole cellular fractions (WCF) (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.

Journal: International Journal of Proteomics

Article Title: A Proteomic Characterization of Bordetella pertussis Clinical Isolates Associated with a California State Pertussis Outbreak

doi: 10.1155/2015/536537

Figure Lengend Snippet: Comparative relative protein abundance profiles for B. pertussis acellular vaccine components. A bar chart illustration to compare normalized total spectra values for each acellular pertussis vaccine component identified in whole cellular fractions (WCF) (diamond bar) versus culture supernatant (CS) (black bar). (a) Filamentous hemagglutinin, pertactin, and serotype fimbriae 2/and 3. (b) Pertussis toxin subunits 1 through 5.

Article Snippet: Whole cellular soluble protein fraction extracts (WCF) used for total proteome and immunoproteome analysis were prepared as described by Bruker Daltonics [ ].

Techniques: Quantitative Proteomics