Comparison

Anti-L-Lactyl-Histone H3 (Lys18) Rabbit mAb (ChIP Grade)

Item no. PTM-1427RM
Manufacturer PTM Biolabs
Amount 100 ul
Format Lyophilized powder
Applications WB, CHIP
Clone PAPTM-599-16
Specific against Human (Homo sapiens), Mouse (Murine, Mus musculus)
Host Rabbit
Isotype IgG
Conjugate/Tag Unconjugated
Alias H3K18la
Shipping condition Room temperature
Available
Manufacturer - Type
Primary Antibodies
Manufacturer - Category
Histone & Histone Modification Antibodies
Manufacturer - Targets
Histone H3
Shipping Temperature
Ambient temperature
Storage Conditions
Store at -20°C. Avoid freeze/thaw cycles.
Molecular Weight
15
Manufacturer - Research Area
Epigenetics
Product description
Malonylation of lysine is a newly identified reversible modification controlling protein activity. Sirt5, a regulatory enzyme for lysine malonylation, can catalyze lysine demalonylation reactions in vivo and in vitro. With integrated proteomic approaches and biochemistry analysis, lysine malonylation is widely distributed in wide ranges of histones and non-histone substrates. Lysine malonylation may provide a new paradigm in the cellular regulation, such as energy metabolism in diverse organisms.
Purification Method
Protein A purified
Manufacturer - Specificity
Anti-L-Lactyl-Histone H3 (Lys18) Rabbit mAb (ChIP Grade) detects histone H3 only when it is L-lactylated at Lys18.
Constituents
PBS, Glycerol, BSA
PTM
Lactyl
Modification Site
Lys18
Immunogen
L-lactylated human histone H3 (Lys18) peptide
Clonality
Recombinant Monoclonal
Stability
Stable for 12 months from date of receipt/reconstitution.
Background
Histones, fundamental proteins involved in chromatin structure and gene regulation, are subject to a wide array of enzyme-catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitination, and numerous others. Histone L-lactylation, a recently discovered post-translational modification induced by lactate has emerged as a significant addition to this repertoire. The extent and dynamics of this modification are highly reliant on lactate levels within the cellular microenvironment and can be modulated through the introduction of extracellular lactate in cultured cells or the stimulation of intracellular glycolysis. The introduction of lysine L-lactylation is mediated by the acetyltransferase p300, while the removal of lactylation marks from histones has been attributed to Class I histone deacetylases (HDAC 1-3). Histone lactylation has been implicated in various biological processes, including inflammation, fibrosis, differentiation, and cancer progression.
Cellular Localization
Nucleus

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 100 ul
Available: In stock
available

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