gradient ipg strip ph3 10 Search Results


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gradient ipg strips  (GE Healthcare)
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GE Healthcare gradient ipg strips
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gradient ipg strip  (Bio-Rad)
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ipg strips  (Bio-Rad)
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Bio-Rad ipg strips
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dimensional electrophoresis  (Bio-Rad)
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Bio-Rad dimensional electrophoresis
Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by <t>2-dimensional</t> <t>electrophoresis</t> (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.
Dimensional Electrophoresis, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ph3 10nl immobiline drystrips  (GE Healthcare)
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GE Healthcare ph3 10nl immobiline drystrips
Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by <t>2-dimensional</t> <t>electrophoresis</t> (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.
Ph3 10nl Immobiline Drystrips, supplied by GE Healthcare, 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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v v ipg buffer  (GE Healthcare)
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GE Healthcare v v ipg buffer
Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by <t>2-dimensional</t> <t>electrophoresis</t> (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.
V V Ipg Buffer, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gradient immobiline drystrip  (GE Healthcare)
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GE Healthcare gradient immobiline drystrip
Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by <t>2-dimensional</t> <t>electrophoresis</t> (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.
Gradient Immobiline Drystrip, supplied by GE Healthcare, 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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ief gel ief page mini ph 3~10  (TEFCO Inc)
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Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by <t>2-dimensional</t> <t>electrophoresis</t> (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.
Ief Gel Ief Page Mini Ph 3~10, supplied by TEFCO Inc, 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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gradient ipg buffer  (GE Healthcare)
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GE Healthcare gradient ipg buffer
Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by <t>2-dimensional</t> <t>electrophoresis</t> (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.
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Image Search Results


Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by 2-dimensional electrophoresis (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Serum Amyloid A Facilitates the Binding of High-Density Lipoprotein From Mice Injected With Lipopolysaccharide to Vascular Proteoglycans

doi: 10.1161/atvbaha.111.226159

Figure Lengend Snippet: Figure 2. MALDI-TOF analysis. HDL (d1.063 to 1.210 g/mL) was isolated by ultracentrifugation from plasma of control and LPS-injected mice. HDL (20 g of protein) was separated by SDS-PAGE (10% to 20% gradient gel), and the gel was stained with Coomassie Brilliant Blue. Each gel band corresponding to the apparent molecular weight of SAA1.1/2.1, SAA4, apoA-I, and apoE was cut out and digested with trypsin, and the pep- tide digest was extracted for tandem mass spectrometric analy- sis by MALDI-TOF. The arrows indicate bands that were identi- fied by MALDI-TOF and database searching that contained peptides unique to SAA1.1/2.1, SAA4, apoA-I, and apoE (A). Albumin-depleted plasma samples (20 L) from control (B-upper panel) and LPS-injected (B-lower panel) mice were separated by 2-dimensional electrophoresis (first dimension: IEF pH 3 to 10; second dimension: 10% SDS-PAGE), and the gel was stained with a silver stain. Selected spots from 2-dimensional gels were identified by in-gel tryptic digest and MALDI-TOF analysis. The small arrows indicate bands that were identified by tandem mass spectrometry MALDI-TOF and database searching that contained peptides unique to SAA1.1 (small arrow B), SAA2.1 (small arrow A), and apoA-I (B). The spot designated SAA2.1 was identified as such with a MASCOT MOWSE score of 374 (CI 100%) (C), and the adjacent spot was identified as SAA1.1 with a MOWSE score of 403 (CI 100%) (D). *Peaks corresponding to SAA peptides.

Article Snippet: Plasma samples (20 μl), from which albumin was removed using Seppro Human Albumin IgY (GenWay Biotech, Inc. San Diego, CA), were separated by two dimensional electrophoresis (first dimension: IEF pH 3-10, second dimension: 10% SDS- PAGE, Bio-Rad Laboratories, Hercules, CA) as per the manufacturer’s instructions.

Techniques: Isolation, Clinical Proteomics, Control, Injection, SDS Page, Staining, Molecular Weight, Electrophoresis, Silver Staining, Mass Spectrometry