acetyltransferase activity kit Search Results


acetyltransferase activity kit  (Enzo Biochem)
90
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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acetyltransferase activity kit - by Bioz Stars, 2026-02
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histone acetyltransferase assay kit  (Active Motif)
90
Active Motif histone acetyltransferase assay 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.
Histone Acetyltransferase Assay Kit, supplied by Active Motif, 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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histone acetyltransferase (hat) activity/inhibition assay kit  (EpiGentek)
90
EpiGentek histone acetyltransferase (hat) activity/inhibition assay 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.
Histone Acetyltransferase (Hat) Activity/Inhibition Assay Kit, supplied by EpiGentek, 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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Average 90 stars, based on 1 article reviews
histone acetyltransferase (hat) activity/inhibition assay kit - by Bioz Stars, 2026-02
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colorimetric histone acetyltransferase activity assay kit  (ScienCell)
90
ScienCell colorimetric histone acetyltransferase activity assay 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.
Colorimetric Histone Acetyltransferase Activity Assay Kit, supplied by ScienCell, 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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Average 90 stars, based on 1 article reviews
colorimetric histone acetyltransferase activity assay kit - by Bioz Stars, 2026-02
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fluorimetric acetyltransferase assay kit  (Active Motif)
90
Active Motif fluorimetric acetyltransferase assay 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.
Fluorimetric Acetyltransferase Assay Kit, supplied by Active Motif, 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/result/fluorimetric acetyltransferase assay kit/product/Active Motif
Average 90 stars, based on 1 article reviews
fluorimetric acetyltransferase assay kit - by Bioz Stars, 2026-02
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histone acetyltransferase (hat) activity assay kit  (Enzo Biochem)
90
Enzo Biochem histone acetyltransferase (hat) activity assay 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.
Histone Acetyltransferase (Hat) Activity Assay 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
https://www.bioz.com/result/histone acetyltransferase (hat) activity assay kit/product/Enzo Biochem
Average 90 stars, based on 1 article reviews
histone acetyltransferase (hat) activity assay kit - by Bioz Stars, 2026-02
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choline acetyltransferase activity assay kit #mbs 2548424  (MyBiosource Biotechnology)
90
MyBiosource Biotechnology choline acetyltransferase activity assay kit #mbs 2548424
(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.
Choline Acetyltransferase Activity Assay Kit #Mbs 2548424, supplied by MyBiosource Biotechnology, 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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Average 90 stars, based on 1 article reviews
choline acetyltransferase activity assay kit #mbs 2548424 - by Bioz Stars, 2026-02
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choline acetyltransferase (chat) activity kit  (Keygen Biotech)
90
Keygen Biotech choline acetyltransferase (chat) 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.
Choline Acetyltransferase (Chat) Activity Kit, supplied by Keygen Biotech, 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/result/choline acetyltransferase (chat) activity kit/product/Keygen Biotech
Average 90 stars, based on 1 article reviews
choline acetyltransferase (chat) activity kit - by Bioz Stars, 2026-02
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Image Search Results


(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