- Antibody Type
- Recombinant monoclonal
- Target
- L-Lactyllysine
- Reactivity
- Human, Mouse, Rat
- Application
- WB, IHC-P, ICC/IF, FC, IP, ChIP
- MW(Calculated)
- Multiple
- MW(Observed)
- Multiple
- Host Species
- Rabbit
- Isotype
- IgG
- Conjugate
- Unconjugated
- Modification
- Lysine lactylation
- Modification Site
- Lys(K)
- Recommended dilution ratio
- WB: 1:500 - 1:1000;IHC-P: 1:200 - 1:1000;ICC/IF: 1:50 - 1:100;FC: 1:50 - 1:100;IP: 1:25 - 1:100;ChIP: 6 μg per 5×10⁶ cells
- Composition
- PBS, Glycerol, BSA
- Purification process
- Protein A
- storageCondition
- Store at -20°C. Avoid repeated freeze-thaw cycles
- Stability
- Stable for 12 months from date of receipt / reconstitution.
- Concentration
- --
- Clonal
- Recombinant monoclonal
- Clone Number
- W-R81
- Immunogen
- polypeptide
- Gene Name
- --
- Protein Name
- --
- Alternative name
- KL-la
- Organism-1
- --
- Gene ID
- --
- SwissProt-1
- --
- --
- Background:
- Background
- L-Lactyllysine (abbreviated as Kla) is a novel lysine acylation-type post-translational modification. It is formed by the covalent attachment of an L-lactyl group to lysine residues, mainly mediated by lactoyl-CoA. Kla is widely distributed on both histone and non-histone proteins, and participates in chromatin remodeling, gene transcription regulation, cellular metabolism, and inflammatory responses. Studies have shown that L-lactylation is closely associated with tumor metabolic reprogramming, hypoxia stress, immune regulation, and various disease processes, serving as a key mechanism linking cellular metabolism and epigenetic regulation.
- Cellular Localization
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- Background:L-Lactyllysine (abbreviated as Kla) is a novel lysine acylation-type post-translational modification. It is formed by the covalent attachment of an L-lactyl group to lysine residues, mainly mediated by lactoyl-CoA. Kla is widely distributed on both histone and non-histone proteins, and participates in chromatin remodeling, gene transcription regulation, cellular metabolism, and inflammatory responses. Studies have shown that L-lactylation is closely associated with tumor metabolic reprogramming, hypoxia stress, immune regulation, and various disease processes, serving as a key mechanism linking cellular metabolism and epigenetic regulation.
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