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Methylated Peptide Synthesis (Peptide Methylation)

Site-defined, homogeneous methylated peptides with defined modification site(s) and stoichiometry (Kme1/Kme2/Kme3, Rme1, ADMA/SDMA). Use PTM panels to map binding specificity, model enzyme “on/off” states, and create reliable assay controls.

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Overview Methylation options Applications Design tips QC & handling FAQ Reading Contact

Overview

Peptide methylation is a post-translational modification (PTM) that regulates molecular recognition, chromatin organization, and signaling through state-specific methyl marks. In synthetic peptides, methylation is most commonly installed on lysine and arginine side chains to generate homogeneous tools for epigenetics, binding assays, and enzyme studies.

Bio-Synthesis provides methylated peptide synthesis with site-defined lysine methylation (Kme1/Kme2/Kme3) and arginine methylation (Rme1, ADMA/SDMA) delivered as homogeneous PTM peptides with controlled stoichiometry, purification, LC–MS/HPLC QC, and COA for epigenetics, reader-domain binding, and methyltransferase/PRMT assay workflows.

Why methylated peptides?
  • Probe reader-domain specificity (chromodomains, Tudor, PHD, etc.)
  • Model defined biological states (Kme3 vs Kme1; ADMA vs SDMA)
  • Support methyltransferase and PRMT enzyme assays
  • Enable clean comparisons with matched unmodified controls
Common applications
  • Histone PTM panels and chromatin biology
  • Protein–protein interaction and binding specificity mapping
  • Antibody validation (state discrimination)
  • Assay calibration, benchmarking, and negative controls

Related PTM services: PTM hub, acetylated peptides,and phosphorylated peptides.

Methylation types we synthesize (site-defined)

Lysine methylation peptides (Kme1/Kme2/Kme3)

Lysine methylation is state-specific—mono-, di-, and trimethyllysine can drive distinct reader interactions and biological outcomes. We synthesize site-defined Kme1/Kme2/Kme3 peptides for epigenetics, chromatin research, and specificity mapping.

  • ε-N-methyllysine (Kme1), ε-N,N-dimethyllysine (Kme2), ε-N,N,N-trimethyllysine (Kme3)
  • Single-site variants and state-ladder panels
  • Matched unmodified controls recommended
Arginine methylation peptides (Rme1, ADMA, SDMA)

Arginine methylation includes mono-methylarginine and dimethyl states that can be asymmetric (ADMA) or symmetric (SDMA). These states are central to PRMT biology and recognition by Tudor-domain proteins.

  • Rme1, ADMA, SDMA at defined arginine positions
  • PRMT substrate peptides and validation controls
  • Compatible with additional PTMs for crosstalk studies
Quick chooser (60 seconds)
Use “methylated PTM peptide” when you need…
  • Biologically faithful methyl marks (native PTMs)
  • State-specific binding (Kme1/Kme2/Kme3; ADMA vs SDMA)
  • Enzyme-state modeling (lysine methyltransferases, PRMTs)
  • Defined stoichiometry and reproducible controls
Use “conjugated / functionalized peptide” when you need…
  • Detection labels (fluorescence, FRET)
  • Capture tags (biotin) or immobilization
  • Handles for assembly (azide/alkyne/DBCO click)
  • Solubility/PK tuning (PEG, lipid payloads)

Not sure which methyl state you need? Tell us your reader domain, antibody, or enzyme assay—we’ll recommend Kme/Rme state(s), controls, and a panel layout.

Methylation state reference (fast)
Residue State Common shorthand Typical use
Lys Monomethyl Kme1 Reader panels; enzyme assays; chromatin studies
Lys Dimethyl Kme2 State-specific recognition; epigenetics; antibody validation
Lys Trimethyl Kme3 High-affinity readers; chromatin marks; specificity mapping
Arg Monomethyl Rme1 PRMT workflows; binding assays; control peptides
Arg Dimethyl (asymmetric) ADMA PRMT biology; Tudor selectivity; assay controls
Arg Dimethyl (symmetric) SDMA PRMT biology; state discrimination; antibody validation

Applications

Epigenetics & chromatin

Histone methylation peptides and PTM panels for chromatin biology, transcriptional regulation, and crosstalk mapping.

Reader-domain binding

Define state-specific binding (Kme1/2/3, ADMA/SDMA) using site-defined methyl marks and matched controls.

Enzyme assays

Substrates and controls for lysine methyltransferases and PRMTs, including state and site variants.

Why synthetic methylated peptides outperform enzymatic mixtures
  • Site-defined methylation and homogeneous composition
  • Controlled stoichiometry across methyl states
  • Matched controls (unmodified and site-variant panels)
  • Ready for quantitative workflows (including optional isotope labeling)

Design tips

Include these in your request
  • Residue type: Lys (Kme) vs Arg (Rme/ADMA/SDMA)
  • Exact residue position(s) and desired methyl state(s)
  • Terminal format (C-terminal acid vs amide)
  • Use case (binding, enzyme assay, LC–MS/MS)
Best-practice panels
  • Methylated vs unmodified peptide pairs
  • State ladder panels (Kme1/Kme2/Kme3; ADMA vs SDMA)
  • Single-site variants to confirm positional specificity
  • Multi-PTM crosstalk sets (methylation + acetylation)

For reader-domain mapping, include a state ladder plus an unmodified control to strengthen conclusions and avoid ambiguous results.

QC & handling

Quality control deliverables
  • Analytical HPLC chromatogram
  • LC–MS confirmation of expected methylation mass shift
  • Certificate of Analysis (COA)
  • PTM panel QC notes (on request)
Handling & stability guidance
  • Storage and aliquoting guidance to minimize freeze–thaw
  • Buffer and pH recommendations for your assay
  • Notes for multi-PTM peptides and long incubations
  • Assay-specific handling (binding vs LC–MS workflows)

Tip: Share assay conditions early (buffer, pH, incubation time, detection method) so we can recommend formats that preserve PTM integrity and reduce redesign cycles.

FAQ

Are methylated peptides synthetic?

Yes. Research-grade methylated peptides are typically chemically synthesized so methylation is installed at defined residue positions and stoichiometry. Synthetic methylated peptides avoid heterogeneity and are preferred for reader-domain studies, enzyme assays, and reproducible controls.

What’s the difference between Kme1, Kme2, and Kme3?

Lysine methylation is state-specific: Kme1 (mono-), Kme2 (di-), and Kme3 (tri-methyllysine) can each produce distinct recognition by reader proteins. State ladder panels help map specificity and avoid false negatives.

What’s the difference between ADMA and SDMA?

Both are dimethylarginine states, but ADMA is asymmetric while SDMA is symmetric. Many binders and antibodies discriminate these states, so including both improves specificity mapping and validation.

Can methylation be combined with acetylation or phosphorylation?

Yes. Methylation is commonly combined with acetylation or phosphorylation to study PTM crosstalk. Tell us your target site(s) and we’ll recommend a panel layout.

More FAQ'sAll FAQ's
Ready to order methylated peptides?

Get site-defined methylated peptide synthesis with controlled stoichiometry across Kme1/Kme2/Kme3 and ADMA/SDMA states—delivered with LC–MS/HPLC QC and COA.

  • Lysine methylation (Kme1 / Kme2 / Kme3)
  • Arginine methylation (Rme1, ADMA, SDMA)
  • Single-site or state-ladder PTM panels

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Not sure which methyl state you need?

Many reader domains, antibodies, and PRMT assays discriminate between Kme1 vs Kme3 or ADMA vs SDMA. Talk with a peptide chemist to avoid ordering the wrong state.

  • Kme state ladder recommendations
  • ADMA vs SDMA guidance
  • Panel design with matched unmodified controls

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Why Choose Bio-Synthesis

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Greetings Researchers,

Please be advised that any information, guidelines, writeups, and oral/video/graphic content on our website are intended solely as general guidelines.
It is the researcher's sole responsibility to conduct thorough research on the designs of the products intended for their experiments before submitting
their designs to Biosynthesis for review of production feasibility.
Thank you for your understanding.

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