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self-assembled monolayer laser desorption-ionization mass spectrometry samdi-ms  (SAMDI Tech)

 
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    SAMDI Tech self-assembled monolayer laser desorption-ionization mass spectrometry samdi-ms
    Self Assembled Monolayer Laser Desorption Ionization Mass Spectrometry Samdi Ms, supplied by SAMDI Tech, 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/laser+desorption+ionization+mass+spectrometry+samdi-ms/self+assembled+monolayer+desorption+ionization+mass+spectrometry+samdi+ms/pm32319753-590-17-22
    Average 90 stars, based on 1 article reviews
    self-assembled monolayer laser desorption-ionization mass spectrometry samdi-ms - by Bioz Stars, 2026-09
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    Mass Spectrometry:

    Article Title: Histones: At the Crossroads of Peptide and Protein Chemistry
    Article Snippet: .. When peptides are immobilized on gold plates covered with a self-assembled monolayer, the resulting arrays can be used in laser desorption ionization mass spectrometry (SAMDI-MS)., Gold surfaces are covered with alkane-thiolates, and subsequently functionalized with maleimide groups. ..



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    Jurkat cells were cultured with or without sugar analogs 1–6 for 72 hours and then incubated <t>with</t> <t>CTxB</t> for 45 min at 4 °C. Cells were photoirradiated, lysed, and the lysates separated by reducing SDS-PAGE followed by protein transfer to PVDF membranes. UV-irradiated (A) and non-UV-irradiated samples (B) were probed for the presence of CTxB (+) using an anti-CTxB antibody. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). The identity of the very low molecular weight band (<10 kDa) is not known, but it appears to be related to a contaminant in the CTxB preparation. UV-irradiated (C) and non-UV-irradiated samples (D) were probed for the presence of GM1a (++) using CTxB-HRP. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). Membranes were stripped and probed for β–actin to demonstrate equal protein loading in each lane (not shown). (E) SAMDI-TOF MS spectrum of <t>SAM-bound</t> monomeric CTxB species derived from cells cultured with Ac4ManNAc, incubated with CTxB, and photoirradiated. (F) SAMDI-TOF MS spectrum of SAM-bound monomeric CTxB and crosslinked CTxB-GM1a-SiaDAz(2me) derived from cells cultured with Ac4ManNDAz(2me), incubated with CTxB, and photoirradiated.
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    Jurkat cells were cultured with or without sugar analogs 1–6 for 72 hours and then incubated <t>with</t> <t>CTxB</t> for 45 min at 4 °C. Cells were photoirradiated, lysed, and the lysates separated by reducing SDS-PAGE followed by protein transfer to PVDF membranes. UV-irradiated (A) and non-UV-irradiated samples (B) were probed for the presence of CTxB (+) using an anti-CTxB antibody. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). The identity of the very low molecular weight band (<10 kDa) is not known, but it appears to be related to a contaminant in the CTxB preparation. UV-irradiated (C) and non-UV-irradiated samples (D) were probed for the presence of GM1a (++) using CTxB-HRP. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). Membranes were stripped and probed for β–actin to demonstrate equal protein loading in each lane (not shown). (E) SAMDI-TOF MS spectrum of <t>SAM-bound</t> monomeric CTxB species derived from cells cultured with Ac4ManNAc, incubated with CTxB, and photoirradiated. (F) SAMDI-TOF MS spectrum of SAM-bound monomeric CTxB and crosslinked CTxB-GM1a-SiaDAz(2me) derived from cells cultured with Ac4ManNDAz(2me), incubated with CTxB, and photoirradiated.
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    Jurkat cells were cultured with or without sugar analogs 1–6 for 72 hours and then incubated with CTxB for 45 min at 4 °C. Cells were photoirradiated, lysed, and the lysates separated by reducing SDS-PAGE followed by protein transfer to PVDF membranes. UV-irradiated (A) and non-UV-irradiated samples (B) were probed for the presence of CTxB (+) using an anti-CTxB antibody. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). The identity of the very low molecular weight band (<10 kDa) is not known, but it appears to be related to a contaminant in the CTxB preparation. UV-irradiated (C) and non-UV-irradiated samples (D) were probed for the presence of GM1a (++) using CTxB-HRP. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). Membranes were stripped and probed for β–actin to demonstrate equal protein loading in each lane (not shown). (E) SAMDI-TOF MS spectrum of SAM-bound monomeric CTxB species derived from cells cultured with Ac4ManNAc, incubated with CTxB, and photoirradiated. (F) SAMDI-TOF MS spectrum of SAM-bound monomeric CTxB and crosslinked CTxB-GM1a-SiaDAz(2me) derived from cells cultured with Ac4ManNDAz(2me), incubated with CTxB, and photoirradiated.

    Journal: Bioconjugate chemistry

    Article Title: Metabolism of diazirine-modified N -acetylmannosamine analogs to photocrosslinking sialosides

    doi: 10.1021/bc2002117

    Figure Lengend Snippet: Jurkat cells were cultured with or without sugar analogs 1–6 for 72 hours and then incubated with CTxB for 45 min at 4 °C. Cells were photoirradiated, lysed, and the lysates separated by reducing SDS-PAGE followed by protein transfer to PVDF membranes. UV-irradiated (A) and non-UV-irradiated samples (B) were probed for the presence of CTxB (+) using an anti-CTxB antibody. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). The identity of the very low molecular weight band (<10 kDa) is not known, but it appears to be related to a contaminant in the CTxB preparation. UV-irradiated (C) and non-UV-irradiated samples (D) were probed for the presence of GM1a (++) using CTxB-HRP. A slower mobility band has an apparent molecular weight consistent with formation of a CTxB-GM1a complex (~13 kDa, *). Membranes were stripped and probed for β–actin to demonstrate equal protein loading in each lane (not shown). (E) SAMDI-TOF MS spectrum of SAM-bound monomeric CTxB species derived from cells cultured with Ac4ManNAc, incubated with CTxB, and photoirradiated. (F) SAMDI-TOF MS spectrum of SAM-bound monomeric CTxB and crosslinked CTxB-GM1a-SiaDAz(2me) derived from cells cultured with Ac4ManNDAz(2me), incubated with CTxB, and photoirradiated.

    Article Snippet: To solidify our assignment of the CTxB-GM1a-SiaDAz(2me) complex, we used self-assembled monolayer (SAM) with matrix-assisted laser desorption/ionization (MALDI) time-of-flight mass spectrometry (denoted SAMDI-TOF-MS) analysis of cell lysates.

    Techniques: Cell Culture, Incubation, SDS Page, Irradiation, Molecular Weight, Derivative Assay