lowess curve set to medium, 10 points in the smoothing window Search Results


90
Esri inc arcgis 10.2
Arcgis 10.2, supplied by Esri 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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99
LI-COR odyssey clx fluorescence scanner
a Small quantities (125 fmol) of CnTagged proteins were mixed with large quantities (~20 µg) of E. coli cell extract and visualized via in-gel <t>fluorescence</t> (left) or with Coomassie (right). The shown proteins are S ingle d omain A nti b ody (SdAb), Ub iquitin (Ub), GroES, G lutathione- S - T ransferase (GST), Ubiquitin-conjugating enzyme (E2), Ubiquitin-activating enzyme (E1), H eat- s hock p rotein 20 kDa (Hsp20), P rotea s o m e subunit A lpha (PsmA), O uter m embrane p hospho l ipase A 1 (OmpLA) and C y clo p hilin A (CyP). The molecular weights and native assembly states of the proteins are indicated. The employed fluorophore-Connectase conjugate (N-Cnt, see control in lane 1) is only visible as a very faint band in presence of CnTagged POI, indicating an effective transfer of the fluorophore. In high-percentage gels, residual fluorescent peptide substrate (~3 kDa) can be seen at the bottom of the gel (see Supplementary Information). Source data are provided as a Source Data file. b Small quantities (125 fmol) of CnTagged E1 protein were mixed with large quantities of Spodoptera frugiperda SF9, human HEK293, Bacillus subtilis , Pseudomonas fluorescens or Sulfolobus solfataricus cell extracts and visualized via in-gel fluorescence (left) or with Coomassie (right). Source data are provided as a Source Data file.
Odyssey Clx Fluorescence Scanner, supplied by LI-COR, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/Odyssey+CLx+Imaging+System/pmc10154401-229-10-14
Average 99 stars, based on 1 article reviews
odyssey clx fluorescence scanner - by Bioz Stars, 2026-10
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90
Menomonee Valley Partners milwaukee river mouth
a Small quantities (125 fmol) of CnTagged proteins were mixed with large quantities (~20 µg) of E. coli cell extract and visualized via in-gel <t>fluorescence</t> (left) or with Coomassie (right). The shown proteins are S ingle d omain A nti b ody (SdAb), Ub iquitin (Ub), GroES, G lutathione- S - T ransferase (GST), Ubiquitin-conjugating enzyme (E2), Ubiquitin-activating enzyme (E1), H eat- s hock p rotein 20 kDa (Hsp20), P rotea s o m e subunit A lpha (PsmA), O uter m embrane p hospho l ipase A 1 (OmpLA) and C y clo p hilin A (CyP). The molecular weights and native assembly states of the proteins are indicated. The employed fluorophore-Connectase conjugate (N-Cnt, see control in lane 1) is only visible as a very faint band in presence of CnTagged POI, indicating an effective transfer of the fluorophore. In high-percentage gels, residual fluorescent peptide substrate (~3 kDa) can be seen at the bottom of the gel (see Supplementary Information). Source data are provided as a Source Data file. b Small quantities (125 fmol) of CnTagged E1 protein were mixed with large quantities of Spodoptera frugiperda SF9, human HEK293, Bacillus subtilis , Pseudomonas fluorescens or Sulfolobus solfataricus cell extracts and visualized via in-gel fluorescence (left) or with Coomassie (right). Source data are provided as a Source Data file.
Milwaukee River Mouth, supplied by Menomonee Valley Partners, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/menomonee+river+basin/pmc06211557__NIHMS979489___supplement___Supplemental_Fig_S3___S13-3-15-27
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milwaukee river mouth - by Bioz Stars, 2026-10
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90
CEM Corporation phm protein content
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Phm Protein Content, supplied by CEM Corporation, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/phm+protein+content/pmc11564000-324-22-12
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86
Keysight Technologies gain setting
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Gain Setting, supplied by Keysight Technologies, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/gain+setting/10__1109_slash_tbcas__2022__3202026-226-24-12
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gain setting - by Bioz Stars, 2026-10
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90
Promega cs-rosetta models
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Cs Rosetta Models, supplied by Promega, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/cs+rosetta+models/pmc02847849-91-4-13
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cs-rosetta models - by Bioz Stars, 2026-10
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90
Biosym Technologies insightii
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Insightii, supplied by Biosym Technologies, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/insightii/pmc02242389-401-15-17
Average 90 stars, based on 1 article reviews
insightii - by Bioz Stars, 2026-10
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90
MBL Life science lc-mbl
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Lc Mbl, supplied by MBL Life 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/product/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/lc+mbl/pm34285341-106-9-2
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90
CAO Group cell-h
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Cell H, supplied by CAO Group, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/cell+h/pmc08563234-369-9-2
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90
Merck KGaA amicon ultra-15 10 kda filter
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Amicon Ultra 15 10 Kda Filter, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/amicon+ultra+centrifugal+filters/pm39893813-130-18-23
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90
CAO Group lignin-h
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Lignin H, supplied by CAO Group, 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/lowess+curve+set+to+medium%2C+10+points+in+the+smoothing+window/lignin+h/pmc08563234-316-10-3
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86
Rajshahi City grain yield
Different formulations of yogurt samples containing varied amount of <t> CEM, </t> CDM and <t> PHM. </t>
Grain Yield, supplied by Rajshahi City, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


a Small quantities (125 fmol) of CnTagged proteins were mixed with large quantities (~20 µg) of E. coli cell extract and visualized via in-gel fluorescence (left) or with Coomassie (right). The shown proteins are S ingle d omain A nti b ody (SdAb), Ub iquitin (Ub), GroES, G lutathione- S - T ransferase (GST), Ubiquitin-conjugating enzyme (E2), Ubiquitin-activating enzyme (E1), H eat- s hock p rotein 20 kDa (Hsp20), P rotea s o m e subunit A lpha (PsmA), O uter m embrane p hospho l ipase A 1 (OmpLA) and C y clo p hilin A (CyP). The molecular weights and native assembly states of the proteins are indicated. The employed fluorophore-Connectase conjugate (N-Cnt, see control in lane 1) is only visible as a very faint band in presence of CnTagged POI, indicating an effective transfer of the fluorophore. In high-percentage gels, residual fluorescent peptide substrate (~3 kDa) can be seen at the bottom of the gel (see Supplementary Information). Source data are provided as a Source Data file. b Small quantities (125 fmol) of CnTagged E1 protein were mixed with large quantities of Spodoptera frugiperda SF9, human HEK293, Bacillus subtilis , Pseudomonas fluorescens or Sulfolobus solfataricus cell extracts and visualized via in-gel fluorescence (left) or with Coomassie (right). Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Specific, sensitive and quantitative protein detection by in-gel fluorescence

doi: 10.1038/s41467-023-38147-8

Figure Lengend Snippet: a Small quantities (125 fmol) of CnTagged proteins were mixed with large quantities (~20 µg) of E. coli cell extract and visualized via in-gel fluorescence (left) or with Coomassie (right). The shown proteins are S ingle d omain A nti b ody (SdAb), Ub iquitin (Ub), GroES, G lutathione- S - T ransferase (GST), Ubiquitin-conjugating enzyme (E2), Ubiquitin-activating enzyme (E1), H eat- s hock p rotein 20 kDa (Hsp20), P rotea s o m e subunit A lpha (PsmA), O uter m embrane p hospho l ipase A 1 (OmpLA) and C y clo p hilin A (CyP). The molecular weights and native assembly states of the proteins are indicated. The employed fluorophore-Connectase conjugate (N-Cnt, see control in lane 1) is only visible as a very faint band in presence of CnTagged POI, indicating an effective transfer of the fluorophore. In high-percentage gels, residual fluorescent peptide substrate (~3 kDa) can be seen at the bottom of the gel (see Supplementary Information). Source data are provided as a Source Data file. b Small quantities (125 fmol) of CnTagged E1 protein were mixed with large quantities of Spodoptera frugiperda SF9, human HEK293, Bacillus subtilis , Pseudomonas fluorescens or Sulfolobus solfataricus cell extracts and visualized via in-gel fluorescence (left) or with Coomassie (right). Source data are provided as a Source Data file.

Article Snippet: The gels were imaged immediately after the run with an Odyssey CLx fluorescence scanner (Licor; 700 nm channel, Intensity: Auto, focus offset: 0.5 mm, resolution: 84–337 µm, quality: lowest-medium).

Techniques: Fluorescence, Control

A serial dilution (from right to left) of CnTagged proteins was detected via in-gel fluorescence, and the normalized densitometric data was plotted. For each protein, three independent experiments (red, green, blue; n = 3) were conducted. The band corresponding to residual N-Cnt is shown for one representative experiment. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Specific, sensitive and quantitative protein detection by in-gel fluorescence

doi: 10.1038/s41467-023-38147-8

Figure Lengend Snippet: A serial dilution (from right to left) of CnTagged proteins was detected via in-gel fluorescence, and the normalized densitometric data was plotted. For each protein, three independent experiments (red, green, blue; n = 3) were conducted. The band corresponding to residual N-Cnt is shown for one representative experiment. Source data are provided as a Source Data file.

Article Snippet: The gels were imaged immediately after the run with an Odyssey CLx fluorescence scanner (Licor; 700 nm channel, Intensity: Auto, focus offset: 0.5 mm, resolution: 84–337 µm, quality: lowest-medium).

Techniques: Serial Dilution, Fluorescence

a Three CnTagged or cMyc-tagged proteins (Actin, SdAb, Ub) were expressed in HEK293 cells. Lysate samples containing the indicated protein quantities were analyzed via in-gel fluorescence or Western blot. (* Ub was detected as a monomer and in conjugates (see Source Data file)). b Three CnTagged or cMyc-tagged proteins (E1, GST, SdAb) were expressed in E. coli and purified. Samples containing the indicated molar protein quantities were analyzed via in-gel fluorescence or Western blot. In-gel fluorescence bands for POI quantities above 10 fmol are equally intense due to the limited amount of used reagent (~6 fmol N-Cnt; see also Fig. ). Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Specific, sensitive and quantitative protein detection by in-gel fluorescence

doi: 10.1038/s41467-023-38147-8

Figure Lengend Snippet: a Three CnTagged or cMyc-tagged proteins (Actin, SdAb, Ub) were expressed in HEK293 cells. Lysate samples containing the indicated protein quantities were analyzed via in-gel fluorescence or Western blot. (* Ub was detected as a monomer and in conjugates (see Source Data file)). b Three CnTagged or cMyc-tagged proteins (E1, GST, SdAb) were expressed in E. coli and purified. Samples containing the indicated molar protein quantities were analyzed via in-gel fluorescence or Western blot. In-gel fluorescence bands for POI quantities above 10 fmol are equally intense due to the limited amount of used reagent (~6 fmol N-Cnt; see also Fig. ). Source data are provided as a Source Data file.

Article Snippet: The gels were imaged immediately after the run with an Odyssey CLx fluorescence scanner (Licor; 700 nm channel, Intensity: Auto, focus offset: 0.5 mm, resolution: 84–337 µm, quality: lowest-medium).

Techniques: Fluorescence, Western Blot, Purification

Different formulations of yogurt samples containing varied amount of  CEM,  CDM and  PHM.

Journal: Food Chemistry: X

Article Title: A comparative study on utilization of different plant-derived nano-mucilage as a fat replacer in yogurt: Product optimization, physicochemical attributes, shelf-life evaluation, and consumer perception with market orientation

doi: 10.1016/j.fochx.2024.101920

Figure Lengend Snippet: Different formulations of yogurt samples containing varied amount of CEM, CDM and PHM.

Article Snippet: Protein content was highest in CDM (4.20 ± 0.08 %), followed by CEM (3.32 ± 0.05 %), and was the lowest in PHM (1.08 ± 0.10 %).

Techniques: Fat

Particle size of spray-dried mucilage (A) CEM, (B) CDM, (C), PHM. ( Colocasia esculenta rhizome mucilage (CEM), Cordia dichotoma fruit mucilage (CDM), and Psyllium husk mucilage (PHM).

Journal: Food Chemistry: X

Article Title: A comparative study on utilization of different plant-derived nano-mucilage as a fat replacer in yogurt: Product optimization, physicochemical attributes, shelf-life evaluation, and consumer perception with market orientation

doi: 10.1016/j.fochx.2024.101920

Figure Lengend Snippet: Particle size of spray-dried mucilage (A) CEM, (B) CDM, (C), PHM. ( Colocasia esculenta rhizome mucilage (CEM), Cordia dichotoma fruit mucilage (CDM), and Psyllium husk mucilage (PHM).

Article Snippet: Protein content was highest in CDM (4.20 ± 0.08 %), followed by CEM (3.32 ± 0.05 %), and was the lowest in PHM (1.08 ± 0.10 %).

Techniques:

Proximate composition of spray-dried  CEM,  CDM, and  PHM.

Journal: Food Chemistry: X

Article Title: A comparative study on utilization of different plant-derived nano-mucilage as a fat replacer in yogurt: Product optimization, physicochemical attributes, shelf-life evaluation, and consumer perception with market orientation

doi: 10.1016/j.fochx.2024.101920

Figure Lengend Snippet: Proximate composition of spray-dried CEM, CDM, and PHM.

Article Snippet: Protein content was highest in CDM (4.20 ± 0.08 %), followed by CEM (3.32 ± 0.05 %), and was the lowest in PHM (1.08 ± 0.10 %).

Techniques: Fat

Syneresis and water holding capacity of formulated yogurt. (A) Syneresis of control samples without addition of mucilage, (B) Syneresis of CEM based yogurt, (C) Syneresis of CDM based yogurt, (D) Syneresis of PHM based yogurt, (E) Water holding capacity of control samples without addition of mucilage, (F) Water holding capacity of CEM based yogurt, (G) Water holding capacity of CDM based yogurt, (H) Water holding capacity of PHM based yogurt. Different error bars represent the standard deviation from the mean values ( n = 3) and lower case (a-d) represent the significantly different among the samples (SKYC, FFYC, SKYPHM5, and MFFYC), Uppercase (A-D) shows the significant difference within the days. (Skimmed yogurt control (SKYC), Full-fat yogurt control (FFYC), Market full-fat yogurt control (MFFYC), PHM: Psyllium husk mucilage.

Journal: Food Chemistry: X

Article Title: A comparative study on utilization of different plant-derived nano-mucilage as a fat replacer in yogurt: Product optimization, physicochemical attributes, shelf-life evaluation, and consumer perception with market orientation

doi: 10.1016/j.fochx.2024.101920

Figure Lengend Snippet: Syneresis and water holding capacity of formulated yogurt. (A) Syneresis of control samples without addition of mucilage, (B) Syneresis of CEM based yogurt, (C) Syneresis of CDM based yogurt, (D) Syneresis of PHM based yogurt, (E) Water holding capacity of control samples without addition of mucilage, (F) Water holding capacity of CEM based yogurt, (G) Water holding capacity of CDM based yogurt, (H) Water holding capacity of PHM based yogurt. Different error bars represent the standard deviation from the mean values ( n = 3) and lower case (a-d) represent the significantly different among the samples (SKYC, FFYC, SKYPHM5, and MFFYC), Uppercase (A-D) shows the significant difference within the days. (Skimmed yogurt control (SKYC), Full-fat yogurt control (FFYC), Market full-fat yogurt control (MFFYC), PHM: Psyllium husk mucilage.

Article Snippet: Protein content was highest in CDM (4.20 ± 0.08 %), followed by CEM (3.32 ± 0.05 %), and was the lowest in PHM (1.08 ± 0.10 %).

Techniques: Control, Standard Deviation