- Antibody Type
- Recombinant monoclonal
- Target
- Butyryllysine
- Reactivity
- Human, Mouse,Rat
- Application
- WB
- MW(Calculated)
- Multiple
- MW(Observed)
- Multiple
- Host Species
- Rabbit
- Isotype
- IgG
- Conjugate
- Unconjugated
- Modification
- Lysine Butyrylation
- Modification Site
- Lys(K)
- Recommended dilution ratio
- WB 1:1000
- Composition
- PBS
- Purification process
- Protein A
- storageCondition
- Upon delivery centrifugate. Reconstitute with 100 μL distilled water (1.0 mg/mL after restoration). Aliquot and store at -80 °C. Avoid freeze / thaw cycles.
- Stability
- Stable for 12 months from date of receipt / reconstitution.
- Concentration
- --
- Clonal
- Recombinant monoclonal
- Clone Number
- W-R19
- Immunogen
- polypeptide
- Gene Name
- --
- Protein Name
- --
- Alternative name
- Kbu
- Organism-1
- --
- Gene ID
- --
- SwissProt-1
- --
- --
- Background:
- Background
- Lysine butyrylation is a newly discovered reversible post-translational modification, which is structurally analogous to lysine acetylation and lysine propionylation and participates in the regulation of protein biological activity. By virtue of integrated proteomic strategies and biochemical analysis, lysine butyrylation has been extensively identified in prokaryotes and eukaryotes, occurring on a large number of substrates including histones and non-histone proteins. Multiple lysine residues of histones and key non-histone proteins such as p53 and p302/CBP can undergo butyrylation modification. Lysine butyrylation exerts essential regulatory functions in epigenetic modulation, mainly by affecting chromatin dynamics and plasticity, mediating DNA transcription regulation, and participating in the occurrence and development of tumorigenesis and other pathological processes.
- Cellular Localization
- --
- --
- Background:Lysine butyrylation is a newly discovered reversible post-translational modification, which is structurally analogous to lysine acetylation and lysine propionylation and participates in the regulation of protein biological activity. By virtue of integrated proteomic strategies and biochemical analysis, lysine butyrylation has been extensively identified in prokaryotes and eukaryotes, occurring on a large number of substrates including histones and non-histone proteins. Multiple lysine residues of histones and key non-histone proteins such as p53 and p302/CBP can undergo butyrylation modification. Lysine butyrylation exerts essential regulatory functions in epigenetic modulation, mainly by affecting chromatin dynamics and plasticity, mediating DNA transcription regulation, and participating in the occurrence and development of tumorigenesis and other pathological processes.
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