Analytical Data
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Gene name
SUV420H2
- Application
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Alternative Names
KMT5C; Lysine N-methyltransferase 5C; Histone-lysine N-methyltransferase SUV420H2
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q6Q783
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Expression Region
Gly2~Leu279
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Molecular Weight
33kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SUV420H2 is a member of the SUV420 family of histone methyltransferases, which play a critical role in the regulation of chromatin structure and gene expression through the methylation of histone tails. Specifically, SUV420H2 is known for its ability to methylate histone H4 at lysine 20 (H4K20), a modification associated with transcriptional repression and heterochromatin formation. Research has shown that dysregulation of SUV420H2 and its methylation activity can lead to various diseases, including cancer, as it influences cell proliferation and differentiation. Given its pivotal role in epigenetic regulation, SUV420H2 has emerged as a potential target for therapeutic intervention. Understanding the structure and function of this protein is essential for developing strategies to modulate its activity, which could aid in reversing pathological gene expression patterns in disease states. Recent studies have focused on characterizing the biochemical properties of SUV420H2, exploring its interaction with other chromatin-associated proteins, and elucidating its catalytic mechanism. The findings from these investigations are not only crucial for basic epigenetics research but also hold significant implications for the development of novel epigenetic therapies aimed at restoring normal gene regulation. As such, the study of SUV420H2 and its recombinant forms represents a promising avenue for research in both fundamental biology and clinical applications.
