PTMScan® Control Peptides Acetyl-Lysine #23068
Product Information
Product Usage Information
Use with Cell Signaling Technology’s PTMScan® kit protocol from the Immunoaffinity Purification (IAP) step. Because the optimal amount of PTMScan® Control Peptides Acetyl-Lysine for each user’s experiments will depend on unique factors such as mass spectrometer sensitivity, users may dilute these control peptides as needed.
1. Aliquot PTMScan® Control Peptides Acetyl-Lysine for storage as single-use units at -20°C or proceed to immediate usage.
2. Resuspend sample peptides in the appropriate buffer and volume, e.g., 1.4 mL of PTMScan® IAP Buffer (1X).
3. Clear sample peptides by centrifugation.
4. Transfer clarified sample peptides to tubes containing IAP beads.
5. Add 10 µL of PTMScan® Control Peptides Acetyl-Lysine to IAP beads and sample peptides and mix well.
6. Continue with PTMScan® or PTMScan® HS workflows at the 2-hour incubation step.
7. Detect PTMScan® Control Peptides Acetyl-Lysine in the LCMS data file.
1. Aliquot PTMScan® Control Peptides Acetyl-Lysine for storage as single-use units at -20°C or proceed to immediate usage.
2. Resuspend sample peptides in the appropriate buffer and volume, e.g., 1.4 mL of PTMScan® IAP Buffer (1X).
3. Clear sample peptides by centrifugation.
4. Transfer clarified sample peptides to tubes containing IAP beads.
5. Add 10 µL of PTMScan® Control Peptides Acetyl-Lysine to IAP beads and sample peptides and mix well.
6. Continue with PTMScan® or PTMScan® HS workflows at the 2-hour incubation step.
7. Detect PTMScan® Control Peptides Acetyl-Lysine in the LCMS data file.
Storage
This product is stable for 24 months when stored at -20°C. Aliquot to avoid multiple freeze/thaw cycles.
Product Description
The PTMScan® Control Peptides Acetyl-Lysine enable quality control of immunoaffinity enrichment performance using PTMScan® or PTMScan® HS workflows. These synthetic peptides contain a specific post-translational modification (PTM) that can be enriched by the associated PTMScan® or PTMScan® HS immunoaffinity purification (IAP) beads, as well as a stable heavy isotope that can be distinguished from endogenous peptides by the mass spectrometer.
Background
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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- Hughes, R.E. (2002) Curr Biol 12, R141-3.
- Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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