PTMScan®N-Terminal Acetyl Motif [N-Ac] Kit #10483
Additional Information
This product is intended for peptide enrichment and mass spectrometry analysis. To learn more about our Proteomics Kits and Services please answer a few questions for our Proteomics group.
Product Information
Product Usage Information
Cells are lysed in a urea-containing buffer, cellular proteins are digested by proteases, and the resulting peptides are purified by reversed-phase, solid-phase extraction. Peptides are then subjected to immunoaffinity purification using a PTMScan® Motif antibody conjugated to protein A agarose beads. Unbound peptides are removed through washing, and the captured PTM-containing peptides are eluted with dilute acid. Reversed-phase purification is performed on microtips to desalt and separate peptides from antibody prior to concentrating the enriched peptides for LC-MS/MS analysis. CST recommends the use of PTMScan® IAP Buffer #9993 included in the kit.
Storage
Antibody beads supplied in IAP buffer containing 50% glycerol. Store at -20°C. Do not aliquot the antibody.
Protocol
Product Description
PTMScan® Technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with liquid chromatography (LC) tandem mass spectrometry (MS/MS) for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. These include phosphorylation (PhosphoScan®), ubiquitination (UbiScan®), acetylation (AcetylScan®), and methylation (MethylScan®), among others. PTMScan® Technology enables researchers to isolate, identify, and quantitate large numbers of post-translationally modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of PTMs in cell and tissue samples without preconceived biases about where these modified sites occur (1). For more information on PTMScan® Proteomics Services, please visit www.cellsignal.com/services/index.html
Background
Various forms of N-terminal protein processing exist in eukaryotes that target the starting methionine amino acid. One such modification is acetylation of the N-terminal methionine accepted from acetyl-CoA. This is mediated by N-terminal acetyltransferases (Nats) and has been found to be present on a wide variety of proteins estimated from 50 to more than 80% of proteins in some cases. There are six identified Nats that are well conserved from yeast to humans (1). This widely observed modification has been implicated in a variety of protein processes from translation regulation, stability, folding, localization, transcriptional control, and protein protein interactions. It also plays a role in Histone tail modifications (2,3,4,5).
限制使用
除非 CST 的合法授书代表以书面形式书行明确同意，否书以下条款适用于 CST、其关书方或分书商提供的书品。 任何书充本条款或与本条款不同的客书条款和条件，除非书 CST 的合法授书代表以书面形式书独接受， 否书均被拒书，并且无效。
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For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
AcetylScan is a registered trademark of Cell Signaling Technology, Inc.
MethylScan is a registered trademark of Cell Signaling Technology, Inc.
PTMScan is a registered trademark of Cell Signaling Technology, Inc.
UbiScan is a registered trademark of Cell Signaling Technology, Inc.
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