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Anti-Mono/Di/Tri-Methyl-Lysine Antibody Conjugated Agarose Beads
Catalog Number: PTM-607
References (1)
$ 1,800

Clone Number: /

Host: Rabbit Clonality: /

Applications: IAP

Reactivity: All

Synonyms: Kme1/2/3

Product Size
500 μl
Quantity

Shipping: Cold packs / Dry ice

Order online or send purchase order to info@ptmbio.com

FAQ Technical Support Protocols

General Information
Isotype IgG
Conjugate Agarose
Synonyms Kme1/2/3
UniProt ID

/

Immunogen Methylated lysine peptides. Further details are proprietary to PTM BIO.
MW (kDa) Multiple
Specificity With high-quality rabbit-derived anti-mono/di/tri-methyl-lysine antibodies cross-linked, this Anti-Mono/Di/Tri-Methyl-Lysine Antibody Conjugated Agarose Beads present extraordinary capability to specifically capture peptides bearing mono-, di-, and tri-methyl lysine residues. This product has been well utilized to affinity purify peptides for global proteomic screening of lysine methylation
Product Usage Information
Applications Dilution Recommended Species
IAP 40 μl beads per 2 mg peptides All
Properties
Purity /
Constituents PBS, Glycerol, BSA
Storage Store at -20°C. Avoid freeze/thaw cycles.
Stability Stable for 12 months from date of receipt/reconstitution.
Target Information

Background

The post-translational ε-amino lysine methylation of proteins is an important reversible modification controlling protein activity. The reversible lysine methylation of proteins plays a vital role in the regulation of many cellular processes including chromatin remodeling, gene expression, cell proliferation, etc. Methylation of lysine residues is modulated by specific counteractive enzymes including lysine methylases (KMTs), demethylases (KDMs), histone methylases (HMTs), and histone demethylases (HDMs), whose pathways have become promising targets for discovery of anti-cancer drugs.

Cellular location

/

Images

Research Use

For research use only, not for use in diagnostic procedures.

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References (1)
  • Protein methylome analysis in Arabidopsis reveals regulation in RNA-related processes
    Year 2020
    Journal J Proteomics
    Authors Qiuju Liang, et al.
    Applications IAP
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