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25 μm 1 d electrode

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The 25 μm I.D. electrode is a specialized lab equipment designed for precise electrochemical measurements. It features a small internal diameter of 25 micrometers, allowing for accurate and localized analyses. The core function of this electrode is to facilitate high-resolution electrochemical experiments and measurements within confined spaces or micro-scale environments.

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Lab products found in correlation

Tripletof 6600 system, by AB Sciex (5 mentions) Nanolc 425 system, by AB Sciex (3 mentions) Chromxp, by AB Sciex (1 mentions)

5 protocols using 25 μm 1 d electrode

1

Quantitative Proteomic Analysis by SWATH-MS

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MS analyses were performed using SWATH®Acquisition on a TripleTOF®6600 System equipped with a DuoSpraySource and 25 μm I.D. electrode (SCIEX). Variable Q1 window SWATH Acquisition methods (100 windows) were built in high sensitivity MS/MS mode with Analyst®TF Software 1.7. Peakgroups from individual runs were statistically scored with pyProphet and all runs were aligned using TRIC to produce a final data matrix. Protein abundances were computed as the sum of the three most abundant peptides (top3 method). After log-transformation and scaling by median count, a linear model was fit to the data. The false discovery rates (FDRs) were estimated using the “p.adjust” function in R. Proteins were considered discriminant when the adjusted p value was below 0.05.
Gertz M.L., Chin C.R., Tomoiaga D., MacKay M., Chang C., Butler D., Afshinnekoo E., Bezdan D., Schmidt M.A., Mozsary C., Melnick A., Garrett-Bakelman F., Crucian B., Lee S.M., Zwart S.R., Smith S.M., Meydan C, & Mason C.E. (2020). Multi-omic, Single-Cell, and Biochemical Profiles of Astronauts Guide Pharmacological Strategies for Returning to Gravity. Cell reports, 33(10), 108429.
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2

Plasma Proteome Profiling by SWATH-MS

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A NanoLC 425 System (SCIEX) was used to separate tryptic peptides of plasma samples. MS analyses were performed with randomized samples using SWATH Acquisition on a TripleTOF 6600 System equipped with a DuoSpray Source and 25 μm I.D. electrode (SCIEX). A final data matrix was produced with 1% FDR at peptide level and 10% FDR at protein level. Protein abundances were computed as the sum of the three most abundant peptides (top3 method). To address batch effects, subtraction of the principal components showing a major batch bias was performed using Perseus (v. 1.4.2.40).
Rose S.M., Contrepois K., Moneghetti K.J., Zhou W., Mishra T., Mataraso S., Dagan-Rosenfeld O., Ganz A.B., Dunn J., Hornburg D., Rego S., Perelman D., Ahadi S., Sailani M.R., Zhou Y., Leopold S.R., Chen J., Ashland M., Christle J.W., Avina M., Limcaoco P., Ruiz C., Tan M., Butte A.J., Weinstock G.M., Slavich G.M., Sodergren E., McLaughlin T.L., Haddad F, & Snyder M.P. (2019). A Longitudinal Big Data Approach for Precision Health. Nature medicine, 25(5), 792-804.
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3

Plasma Proteome Profiling by SWATH-MS

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Tryptic peptides of plasma samples were separated on a NanoLC 425 System (SCIEX). The flow was 5 μl/min with trap-elute setting using a 0.5 × 10 mm ChromXP (SCIEX). The LC gradient was set to a 43-min gradient from 4–32% B with 1 h total run. Mobile phase A was 100% water with 0.1% formic acid. Mobile phase B was 100% acetonitrile with 0.1% formic acid. We used an 8-μg load of undepleted plasma on a 15-cm ChromXP column. MS analysis was performed using SWATH acquisition on a TripleTOF 6600 system equipped with a DuoSpray source and 25-μm ID electrode (SCIEX). Variable Q1 window SWATH Acquisition methods (100 windows) were built in high-sensitivity MS/MS mode with Analyst TF Software 1.7.
Zhou W., Sailani M.R., Contrepois K., Zhou Y., Ahadi S., Leopold S.R., Zhang M.J., Rao V., Avina M., Mishra T., Johnson J., Lee-McMullen B., Chen S., Metwally A.A., Tran T.D., Nguyen H., Zhou X., Albright B., Hong B.Y., Petersen L., Bautista E., Hanson B., Chen L., Spakowicz D., Bahmani A., Salins D., Leopold B., Ashland M., Dagan-Rosenfeld O., Rego S., Limcaoco P., Colbert E., Allister C., Perelman D., Craig C., Wei E., Chaib H., Hornburg D., Dunn J., Liang L., Rose S.M., Kukurba K., Piening B., Rost H., Tse D., McLaughlin T., Sodergren E., Weinstock G.M, & Snyder M. (2019). Longitudinal multi-omics of host–microbe dynamics in prediabetes. Nature, 569(7758), 663-671.
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4

Quantitative Proteomic Analysis by SWATH-MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
MS analyses were performed using SWATH®Acquisition on a TripleTOF®6600 System equipped with a DuoSpraySource and 25 μm I.D. electrode (SCIEX). Variable Q1 window SWATH Acquisition methods (100 windows) were built in high sensitivity MS/MS mode with Analyst®TF Software 1.7. Peakgroups from individual runs were statistically scored with pyProphet and all runs were aligned using TRIC to produce a final data matrix. Protein abundances were computed as the sum of the three most abundant peptides (top3 method). After log-transformation and scaling by median count, a linear model was fit to the data. The false discovery rates (FDRs) were estimated using the “p.adjust” function in R. Proteins were considered discriminant when the adjusted p value was below 0.05.
Gertz M.L., Chin C.R., Tomoiaga D., MacKay M., Chang C., Butler D., Afshinnekoo E., Bezdan D., Schmidt M.A., Mozsary C., Melnick A., Garrett-Bakelman F., Crucian B., Lee S.M., Zwart S.R., Smith S.M., Meydan C, & Mason C.E. (2020). Multi-omic, Single-Cell, and Biochemical Profiles of Astronauts Guide Pharmacological Strategies for Returning to Gravity. Cell reports, 33(10), 108429.
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5

Plasma Proteome Profiling by SWATH-MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
A NanoLC 425 System (SCIEX) was used to separate tryptic peptides of plasma samples. MS analyses were performed with randomized samples using SWATH Acquisition on a TripleTOF 6600 System equipped with a DuoSpray Source and 25 μm I.D. electrode (SCIEX). A final data matrix was produced with 1% FDR at peptide level and 10% FDR at protein level. Protein abundances were computed as the sum of the three most abundant peptides (top3 method). To address batch effects, subtraction of the principal components showing a major batch bias was performed using Perseus (v. 1.4.2.40).
Rose S.M., Contrepois K., Moneghetti K.J., Zhou W., Mishra T., Mataraso S., Dagan-Rosenfeld O., Ganz A.B., Dunn J., Hornburg D., Rego S., Perelman D., Ahadi S., Sailani M.R., Zhou Y., Leopold S.R., Chen J., Ashland M., Christle J.W., Avina M., Limcaoco P., Ruiz C., Tan M., Butte A.J., Weinstock G.M., Slavich G.M., Sodergren E., McLaughlin T.L., Haddad F, & Snyder M.P. (2019). A Longitudinal Big Data Approach for Precision Health. Nature medicine, 25(5), 792-804.
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