elisa analysis using a kit and protocol provided by novus biologicals Search Results


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Inositol Phosphate One Elisa Kit, supplied by Cisbio Bioassays, 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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Enzo Biochem acetyltransferase activity kit
(A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and <t>acetyltransferase</t> assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.
Acetyltransferase Activity Kit, supplied by Enzo Biochem, 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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Corbett Life Science rotergene 3000 thermal cycling instrument
(A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and <t>acetyltransferase</t> assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.
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Immuno-Biological Laboratories Co Ltd elisa kits
(A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and <t>acetyltransferase</t> assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.
Elisa Kits, supplied by Immuno-Biological Laboratories Co Ltd, 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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Morinaga Institute of Biological Science eia kit
(A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and <t>acetyltransferase</t> assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.
Eia Kit, supplied by Morinaga Institute of Biological Science, 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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Thermo Fisher revertaidtm h minus kits
(A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and <t>acetyltransferase</t> assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.
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(A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and acetyltransferase assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.

Journal: The Biochemical journal

Article Title: N-terminal acetylation and methylation differentially affect the function of MYL9

doi: 10.1042/BCJ20180638

Figure Lengend Snippet: (A) WT MYL9 (SSK) has been found in Nα-methylated and Nα-acetylated forms. The S3P (SPK) MYL9 mutant is Nα-methylated, and the K4Q (SSQ) MYL9 mutant is Nα-acetylated. In vivo, the initiator methionine of WT MYL9 is cleaved to reveal the N-terminal sequence shown. (B–G) in vitro methyltransferase and acetyltransferase assays were performed to determine the KM of NRMT1 or NAA10 (the catalytic subunit of NatA) when using peptides corresponding to the 14 N-terminal amino acids (after Met cleavage) of WT and mutant MYL9 as substrates. (B) The KM of NRMT1 with WT (SSK) MYL9 was determined to be 28.8 μM. (C) NAA10 with WT (SSK) MYL9 had a KM of 0.7 μM. (D) SPK MYL9 was confirmed to be a preferred substrate of NRMT1 with a KM of 0.7 μM. (E) NAA10 showed no activity with SPK MYL9 up to 40 μM. (F) SSQ MYL9 Figure 1. N-terminal mutants of MYL9 select for Nα-methylation or Nα-acetylation. Part 2 of 2 was not a substrate of NRMT1, showing no activity up to 160 μM. (G) The KM of NAA10 with SSQ MYL9 was 5.0 μM. n = 3 for all experiments. All error bars represent standard deviation.

Article Snippet: In vitro acetyltransferase experiments were performed using the Enzo Acetyltransferase Activity Kit (Enzo Life Sciences, Farmingdale, NY) following manufacturer guidelines.

Techniques: Methylation, Mutagenesis, In Vivo, Sequencing, In Vitro, Activity Assay, Standard Deviation