Analytical Data
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Gene name
MLL4
- Application
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Alternative Names
Histone-lysine N-methyltransferase 2B. Lysine N-methyltransferase 2B. EC:2.1.1.364. Myeloid/lymphoid or mixed-lineage leukemia protein 4. Trithorax homolog 2. WW domain-binding protein 7. WBP-7
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UMN6
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Expression Region
1487-1586 aa
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AA Sequence
SKLEGMFPAYLQEAFFGKELLDLSRKALFAVGVGRPSFGLGTPKAKGDGGSERKELPTSQKGDDGPDIADEESRGLEGKADTPGPEDGGVKASPVPSDPE
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Molecular Weight
36.74 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
MLL4, also known as KMT2D, is a critical member of the MLL family of histone methyltransferases, playing a significant role in the regulation of gene expression through histone modification. Mutations and dysregulation of MLL4 have been linked to several types of cancers, particularly in pediatric acute lymphoblastic leukemia and other hematological malignancies. The importance of MLL4 in normal hematopoiesis and its role as a tumor suppressor make it a compelling target for cancer research. Understanding the biochemical mechanisms by which MLL4 exerts its effects on chromatin remodeling and gene expression is essential for developing targeted therapies. Recent studies focus on producing recombinant MLL4 protein to investigate its enzymatic activity, interaction with other regulatory proteins, and impact on chromatin architecture. These investigations not only enhance our understanding of MLL4's role in oncogenesis but also pave the way for potential therapeutic strategies aimed at restoring normal function in MLL4-deficient cancers. Continued research into the structure-function relationship of MLL4 and its associated complexes promises to provide deeper insights into its biological significance and therapeutic potential.
