[Lys(Me2)36]-Histone H3 (31-41)

[Lys(Me2)36]-Histone H3 (31-41)

For laboratory research purposes only. Not for human or veterinary use.

Purity: 95%

CAT.NO: P400434

Categories: , ,

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Description

Product Name: [Lys(Me2)36]-Histone H3 (31-41)

Sequence One Letter Code: STGGV-K(Me2)-KPHRY

Sequence Three Letter Code: H-Ser-Thr-Gly-Gly-Val-Lys(Me2)-Lys-Pro-His-Arg-Tyr-OH

Molecular Weight: 1257.5

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: [Lys(Me2)36]-Histone H3 (31–41) is a synthetic peptide corresponding to histone H3 residues 31–41 with site-specific dimethylation at lysine 36 (H3K36me2). This epigenetic modification is associated with transcriptional elongation, chromatin organization, and regulation of alternative splicing. H3K36me2 plays an important role in maintaining genomic stability and controlling gene expression across actively transcribed regions. It is also involved in recruiting chromatin-modifying enzymes and regulating histone–DNA interactions. This peptide is widely used in epigenetics research to study histone methyltransferase activity, chromatin-binding proteins, and transcriptional regulation mechanisms. It is suitable for binding assays, enzyme studies, and functional analysis of histone modifications in gene expression and chromatin dynamics.

Current Research: Epigenetic modifications of histone proteins are central to the regulation of gene expression and chromatin structure. Among these, dimethylation of lysine 36 on histone H3 (H3K36me2) is an important modification associated with actively transcribed chromatin regions. [Lys(Me2)36]-Histone H3 (31–41) is a synthetic peptide designed to replicate this specific epigenetic mark within a defined segment of histone H3, providing a valuable tool for investigating transcriptional regulation, chromatin organization, and histone methylation–dependent signaling pathways. Biological Role of H3K36 Dimethylation H3K36 methylation exists in multiple states—mono-, di-, and trimethylation—each contributing to distinct regulatory functions. H3K36me2 is broadly distributed across gene bodies and intergenic regions and is closely linked to transcriptional elongation. It helps maintain chromatin in a state that supports active transcription while preventing aberrant initiation from cryptic promoters. This modification also plays a role in: Regulation of alternative splicing, influencing exon selection during mRNA processing Chromatin organization, contributing to proper nucleosome positioning Maintenance of genomic stability, particularly during DNA replication and repair By marking actively transcribed regions, H3K36me2 helps coordinate transcription with downstream RNA processing and chromatin maintenance mechanisms. Structural Design of the Peptide The [Lys(Me2)36]-Histone H3 (31–41) peptide corresponds to amino acids 31–41 of the histone H3 sequence, encompassing the region surrounding lysine 36. In this synthetic construct, lysine 36 is specifically dimethylated, faithfully reproducing the H3K36me2 modification observed in vivo. This short, defined peptide format allows researchers to isolate the effects of a single histone modification without interference from additional epigenetic marks. As a result, it provides a controlled system for studying how H3K36me2 influences protein binding, chromatin interactions, and transcriptional processes. Role in Chromatin Signaling and Protein Recruitment Histone methylation marks function as signals that recruit chromatin-associated proteins with specialized recognition domains. H3K36me2 is known to interact with proteins involved in transcription regulation, chromatin remodeling, and RNA processing. These interactions contribute to: Coordination of transcriptional elongation with chromatin structure Recruitment of histone-modifying enzymes that further shape chromatin states Regulation of histone–DNA interactions, influencing nucleosome stability Through these mechanisms, H3K36me2 acts as a key mediator linking transcriptional activity with chromatin dynamics. Applications in Epigenetics and Chromatin Research Because it reproduces a biologically relevant histone modification, [Lys(Me2)36]-Histone H3 (31–41) is widely used in studies focused on epigenetic regulation and transcriptional control. Typical applications include: Histone methyltransferase activity assays to study enzymes that regulate H3K36 methylation Protein–peptide interaction studies to identify H3K36me2-binding proteins Chromatin-binding assays involving transcription-associated complexes Biochemical studies of transcriptional elongation mechanisms Functional analysis of histone modifications in gene expression These approaches allow researchers to dissect how histone methylation contributes to gene regulation at the molecular level. H3K36me2 in Genome Stability and Disease H3K36 methylation plays a critical role in preserving genomic integrity. It is involved in DNA repair pathways and helps ensure accurate transcription and replication. Disruption of H3K36 methylation patterns has been linked to genomic instability and disease, including cancer. Mutations in enzymes responsible for H3K36 methylation, such as NSD family methyltransferases, can alter chromatin states and lead to abnormal gene expression. These changes are associated with various malignancies and developmental disorders, highlighting the importance of this modification in maintaining normal cellular function. A Valuable Tool for Studying Transcription and Chromatin Dynamics Synthetic histone peptides provide precise models for investigating the complex mechanisms of epigenetic regulation. By faithfully replicating the H3K36 dimethylation mark, [Lys(Me2)36]-Histone H3 (31–41) enables detailed analysis of how histone modifications influence transcriptional elongation, chromatin organization, and RNA processing. Through applications in binding assays, enzyme studies, and chromatin research, this peptide supports advances in understanding gene expression control, epigenetic signaling pathways, and the role of histone methylation in development and disease.

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