Analytical Data
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Gene name
KMT2E
- Application
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Alternative Names
KMT2E；MLL5；Inactive histone-lysine N-methyltransferase 2E
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IZD2
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Expression Region
151-450aa
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AA Sequence
RQHIPDTYLCERCQPRNLDKERAVLLQRRKRENMSDGDTSATESGDEVPVELYTAFQHTPTSITLTASRVSKVNDKRRKKSGEKEQHISKCKKAFREGSRKSSRVKGSAPEIDPSSDGSNFGWETKIKAWMDRYEEANNNQYSEGVQREAQRIALRLGNGNDKKEMNKSDLNTNNLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDY
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Molecular Weight
42.2 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
Related Products
Protein Description
KMT2E, also known as MLL4, is a member of the mixed-lineage leukemia (MLL) family of proteins that function as histone methyltransferases, playing a crucial role in chromatin remodeling and gene expression regulation. Its significance has been increasingly recognized in the context of various cancers, particularly those arising from alterations in epigenetic regulation. Research suggests that KMT2E is involved in maintaining stem cell pluripotency and differentiation pathways, making it a subject of interest in developmental biology and cancer therapeutics. The study of KMT2E recombinant proteins has emerged as a valuable approach to elucidate its biochemical properties and functional mechanisms. By generating and purifying KMT2E recombinant proteins, researchers can investigate their enzymatic activity, substrate specificity, and interactions with other epigenetic regulators. This research could reveal insights into the pathological mechanisms underlying KMT2E-related malignancies and potentially identify novel therapeutic targets. Understanding the structure-function relationship of KMT2E through recombinant protein studies is essential for the development of inhibitors or modulators that could correct aberrant KMT2E activity in cancer cells. Overall, the study of KMT2E recombinant proteins is a promising area of research that could lead to advancements in our understanding of epigenetic regulation and cancer biology.
