Acetyl lysine Specific Antibody Conjugated Agarose Beads
Product details
Acetyllysine Specific Antibody Conjugated Agarose Beads is an immunoaffinity enrichment tool for acetyllysine peptides in mass spectrometry-based proteomics. The highly specific antibody selectively captures target modified peptides without cross-reactivity, is applicable to all species, efficiently enriches low-abundance peptides and reduces background interference, delivering stable and reliable results for acetyllysine modification research.
Specifications
| Target | Acetyllysine |
| Reactivity | Species Independent |
| Application | IAC, IAP, IP |
| MW(Calculated) | |
| MW(Observed) | |
| Host Species | |
| Isotype | |
| Conjugate | Agarose Beads |
| Modification | Lysine lactylation |
| Modified site | Lys(K) |
| Recommended dilution ratio | |
| Composition | |
| Purification process | Protein A |
| Purity | |
| Storage | 50% slurry in PBS pH7.4, 0.05% Proclin 300. Ensure thorough mixing before each use. Wide-mouth pipette tips are recommended. In case of difficulty in aspiration due to improper operation, additional Storage Buffer can be added at your discretion. |
| Stability | 12 months from date of receipt / reconstitution, 2 to 8 °C as supplied |
| Clonal | Recombinant monoclonal |
| Clone Number | |
| Immunogen | |
| Sequence | |
| Specificity | |
| Gene name | |
| Protein Name | |
| Alternative name | Kac |
| Organism-1 | |
| GeneID-1 | |
| SwissProt-1 | |
| Organism-2 | |
| GeneID-2 | |
| SwissProt-2 | |
| Organism-3 | |
| GeneID-3 | |
| SwissProt-3 | |
| Organism-4 | |
| GeneID-4 | |
| SwissProt-4 | |
| Background | Acetyllysine (abbreviated as Kac) is a classic and widespread post-translational modification of lysine acetylation. This modification covalently adds an acetyl group to the side-chain amino group of lysine residues, altering the charge and structure of proteins to regulate their functions. Lysine acetylation is an important epigenetic marker on histones, involved in chromatin remodeling and gene transcription regulation. It also widely exists in non-histone proteins such as metabolic enzymes, signaling proteins, and transcription factors, playing essential roles in cellular metabolism, signal transduction, cell cycle progression, and DNA repair. Dysregulation of lysine acetylation is closely associated with the development of cancer, metabolic diseases, neurodegenerative diseases, and other disorders. |
| Cellular Localization |
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