| Product Includes | Volume (with Count) | ||||
|---|---|---|---|---|---|
| PTMScan® Acetyl-Lysine Motif [Ac-K] Immunoaffinity Beads | 3 x 80 µl | ||||
| PTMScan® IAP Buffer (10X) 9993 | 3 x 600 µl | ||||
| PTMScan® Trypsin Digested Control Peptides I 12219 | 1 x 1 vial |
Product 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. A detailed protocol and Limited Use License allowing the use of the patented PTMScan® method are included with the kit.
PTMScan® Trypsin Digested Control Peptides I are supplied as lyophilized powder. Centrifuge the tube containing the lyophilized peptide in order to collect all material to be dissolved. Add 1.4 ml PTMScan® IAP Buffer (1X) and follow the PTMScan® kit protocol from the Immunoaffinity Purification (IAP) step using the entire vial of reconstituted peptides.
Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. The conserved amino-terminal domains of the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (1). Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis (2-6). Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of post-translational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport (7,8). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (9), and HDACs have become promising targets for anti-cancer drugs currently in development (10).
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![PTMScan® Pilot Acetyl-Lysine Motif [Ac-K] Kit: Image 1](http://media.cellsignal.com/product/image/14499_fig02___20210423082605.jpg)
![PTMScan® Pilot Acetyl-Lysine Motif [Ac-K] Kit: Image 2](http://media.cellsignal.com/product/image/14499_fig03___20210423082356.jpg)