Pan Dimethyl Antibody
Pan Dimethyl Antibody - Related Videos
02:35
Long-Term Cryopreservation of Cyanobacterial Strains Using Glycerol or Dimethyl Sulfoxide
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2025
Source: Lea-Smith, D. J., et al. Generation of Marked and Markerless Mutants in Model Cyanobacterial Species. J. Vis. Exp. (2016)This video demonstrates the cryopreservation of cyanobacterial strains by combining concentrated cell suspensions with glycerol or DMSO and storing them at low temperatures, enabling long-term maintenance of viable cultures for photosynthesis and genetic studies.
13:59
Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Cited by 4 •
2013
Two methods for assigning the α- and ε-dimethylamine nuclear magnetic resonance signals of a reductively 13C-methylated N-terminal lysine are described. One method utilizes the pH-induced selectivity of the reductive methylation reaction, and the other uses aminopeptidase to selectively remove the N-terminal lysine.
13:45
Using a Pan-Viral Microarray Assay (Virochip) to Screen Clinical Samples for Viral Pathogens
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Cited by 84 •
2011
The Virochip is a pan-viral microarray designed to simultaneously detect all known viruses as well as novel viruses on the basis of conserved sequence homology. Here we demonstrate how to run a Virochip assay to analyze clinical samples for the presence of both known and unknown viruses.
12:28
Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
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Cited by 8 •
2016
We provide a method to simultaneously screen a library of antibody fragments for binding affinity and cytoplasmic solubility by using the Escherichia coli twin-arginine translocation pathway, which has an inherent quality control mechanism for intracellular protein folding, to display the antibody fragments on the inner membrane.
11:53
Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
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Cited by 38 •
2014
Stable isotope labeling of peptides by reductive dimethylation (ReDi labeling) is a rapid, inexpensive strategy for accurate mass spectrometry-based quantitative proteomics. Here we demonstrate a robust method for preparation and analysis of protein mixtures using the ReDi approach that can be applied to nearly any sample type.
FAQs
Recognition depends on the dimethylated epitope, not primarily on the identity of a single protein. The antibody binds proteins that present the relevant dimethylated residue, most commonly dimethyl lysine, so one measurement can reflect methylation across multiple cellular proteins. This broad binding behavior enables global methylation profiling.
A protein-specific antibody answers whether one selected protein is present or modified, whereas a Pan Dimethyl Antibody surveys dimethylation across the proteins represented in the sample. That broader view is useful when the relevant methylated targets are unknown or when researchers want to compare overall methylation states instead of tracking one predefined protein.
Dimethyl lysine is important because it is the residue most commonly recognized by this broad-spectrum reagent. Detecting it in histones and other cellular proteins allows researchers to examine methylation patterns across distinct protein groups. Those patterns can then be related to gene regulation, tumor progression, or treatment response.
Changes in antibody signal can be used to assess the activity or selectivity of treatments designed to target methyltransferases. A decrease or shift under an experimental condition may indicate altered global methylation, but the readout represents dimethylated proteins collectively rather than a single defined target. Comparing conditions therefore helps evaluate treatment-associated epigenetic changes.
Immunoblotting, immunoprecipitation, and related immunoassays can use this reagent to detect dimethylated proteins. These formats support analysis of methylation signals in experimental samples, while the broad recognition profile keeps the focus on aggregate protein methylation rather than one predetermined protein. That makes the antibody adaptable to global profiling in cancer-related studies.
Researchers can compare dimethylation patterns across tumors, cell lines, or experimental conditions using the same broad recognition principle. Such comparisons reveal whether global methylation differs between biological contexts or changes after an intervention. In cancer research, the resulting patterns help characterize epigenetic states and relate them to tumor progression or therapeutic response.
By measuring dimethylated proteins before and after an experimental treatment, researchers can assess whether a methyltransferase-targeting intervention changes the broader methylation profile. Comparisons across conditions may also help evaluate selectivity, especially when treatment effects are considered alongside signals from histones and other cellular proteins. The result is a readout of treatment-associated epigenetic change.
Because recognition is broad, a positive signal does not identify one specific methylated protein or establish which protein drives an observed cancer-related outcome. The measurement is therefore most informative as a global methylation profile that can be compared across samples or treatments. Researchers can use those patterns to support interpretation of gene regulation, progression, or response.