Anti-Pan-Acetyl-Lysine antibody [SMM5007] (STJ11106167)
SPECIFICATIONS
ClonalityMonoclonal
HostMouse
ConjugationUnconjugated
IsotypeIgG1
General Information
| Short Description | Mouse monoclonal Pan-Acetyl-Lysine antibody for use in WB and ELISA in human, mouse, rat and other samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | WB/ELISA |
| Host | Mouse |
| Reactivity | Human/Mouse/Rat/Other |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Monoclonal |
| Clone ID | SMM5007 |
| Isotype | IgG1 |
| Conjugation | Unconjugated |
| Concentration | Lot specific |
| Purification | Affinity purification |
| Dilution Range | WB:1:500-1:1000ELISA:Recommended starting concentration is 1 Mu g/mL. Please optimize the concentration based on your specific assay requirements. |
| Formulation | PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. |
Target Information
| Specificity | Recombinant fusion protein corresponding to a sequence containing acetylated K. |
Additional Info
| 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) (PMID: 9667866). 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 (PMID: 14593721). 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 (PMID: 19608861). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (PMID: 11864588) , and HDACs have become promising targets for anti-cancer drugs currently in development (PMID: 15032670). |
Information sourced from Uniprot.org