Acetyl Lys proteins rabbit pAb
AO-06-ES4384-100
| ELK.No | ES4384 |
| Product name | Acetyl Lys proteins rabbit pAb |
| Reactivity | Human;Mouse;Rat;Monkey,plant |
| Applications | WB;IHC;IF;ELISA |
| Other name | |
| Size | 100μL |
| Unit price ($) | 248 |
| Human gene ID | |
| Human Swiss-Prot | |
| Source | Rabbit |
| Isotype | IgG |
| Target | Acetyl Lys proteins |
| Fields | |
| Gene name | |
| Protein name | |
| Human gene link | |
| Human Swiss link | |
| Mouse gene ID | |
| Mouse gene link | |
| Mouse Swiss-Prot | |
| Mouse Swiss link | |
| Rat gene ID | |
| Rat gene link | |
| Rat Swiss-Prot | |
| Rat Swiss link | |
| Immunogen | Synthesized acetyl-peptide derived from human acetylation Lys proteins. |
| Specificity | Acetyl-Lys proteins Polyclonal Antibody detects endogenous levels of acetylated Lys proteins. |
| Formulation | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. |
| Clonality | Polyclonal |
| Dilution | Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. Immunofluorescence: 1/200 - 1/1000. ELISA: 1/10000. Not yet tested in other applications. |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. |
| Concentration | 1 mg/ml |
| Storage stability | -20°C/1 year |
| Molecular Weight (Da) | |
| Observed band (KD) | 20,40,80,175kD |
| 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). 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. 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. The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development. |
| Function | |
| Subcellular location | |
| Expression |



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