Product Pathways - Motif Antibodies
PTMScan® Acetyl-Lys Motif (Ac-K) Immunoaffinity Beads
| Consenus Site | Cell or Tissue Type | Study No. | Modified Peptides Identified |
|---|---|---|---|
| Ac-K | Jurkat (T cell acute lymphoblastic leukemia) | 2292 | 283 |
Services Information
This product is not for individual sale. It is only available as a component of the PTMScan® Proteomics System. PTMScan® Proteomics System orders must be priced out individually. Please email us at ptmscan@cellsignal.com to receive the most accurate pricing.
Description
PTMScan® Immunoaffinity Beads are custom preparations of motif antibodies coupled to protein A beads. They are intended only for use for PTMScan® and are available as components of the PTMScan® Proteomics System.
Specificity / Sensitivity
PTMScan® Acetyl-Lys Motif (Ac-K) Immunoaffinity Beads detect and capture endogenous levels of peptide derived from protease digested cellular proteins modified by acetylation on the epsilon-amine groups of lysine residues. The antibody recognizes acetylated lysine in a wide range of sequence contexts. (U.S. Patent No's.: 6,441,140; 6,982,318; 7,259,022; 7,344,714; U.S.S.N. 11,484,485; and all foreign equivalents.)
Western Blotting
Western blot analysis of extracts from HCT-116 cells, untreated or treated with trichostatin A (TSA), using an Acetylated Lysine Rabbit mAb, the unconjugated antibody corresponding to PTMScan® Acetyl-Lys Motif (Ac-K) Immunoaffinity Beads.
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 posttranslational 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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Application References
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
For Research Use Only. Not For Use In Diagnostic Procedures.
