Analytical Data
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Gene name
DOT1L
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简介
The DOT1L protein, a histone methyltransferase, methylates lysine-79 of histone H3. It shows high activity against nucleosomes but not free core histones. It is broadly expressed, particularly in tissues like the testis, bone marrow, and 22 other tissues. DOT1L Protein, Human is the recombinant human-derived DOT1L protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
Histone H3-K79 methyltransferase; H3-K79-HMTase; DOT1L; KIAA1814; KMT4
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TEK3-1
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Expression Region
G2-K416
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Protein Length
Partial
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Molecular Weight
50 kDa
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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
DOT1L (Disruptor of TEL-OMYELoblastoma 1) is a histone methyltransferase that specifically tri-methylates lysine 79 on histone H3 (H3K79me3), playing a critical role in regulating gene expression, DNA repair, and cell differentiation. Its significance has been underscored by its involvement in various cancers, particularly acute leukemias, where DOT1L-mediated H3K79 methylation contributes to oncogenic gene activation. Overexpression or mutations in DOT1L have been associated with poor prognosis, making it a pertinent target for therapeutic intervention. Research has increasingly focused on understanding the molecular mechanisms by which DOT1L exerts its effects, as well as the development of potent inhibitors that might disrupt its activity. The ability to produce and purify recombinant DOT1L is pivotal for these studies, enabling investigations into its enzymatic properties, substrate specificity, and interactions with other proteins. Advances in structural biology have provided insights into the enzyme's active site and substrate recognition, propelling efforts to develop small-molecule inhibitors that can effectively block its function in disease contexts. As a result, DOT1L has emerged as a promising target for novel treatments in oncology, highlighting the importance of understanding its biochemical and functional properties through the study of its recombinant forms.
