Analytical Data
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Gene name
DPY30
- Application
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Alternative Names
DPY30;Protein dpy-30 homolog
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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
Q9C005
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Expression Region
2-99aa
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AA Sequence
EPEQMLEGQTQVAENPHSEYGLTDNVERIVENEKINAEKSSKQKVDLQSL PTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN
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Molecular Weight
12 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
The DPY30 protein, a crucial component of the histone methyltransferase complex, has garnered significant attention in the field of epigenetics due to its role in gene regulation and chromatin remodeling. As a member of the Dpy-30-like family, DPY30 participates in the formation of the MLL (Mixed Lineage Leukemia) complex, which is involved in the mono- and tri-methylation of histone H3 at lysine 4 (H3K4), marking active transcription and ensuring proper gene expression during development and cellular differentiation. Research has indicated that abnormalities in DPY30 function can lead to various diseases, including cancers and other developmental disorders. Understanding the structure and function of DPY30, particularly through the study of its recombinant protein forms, has become essential for elucidating its precise role in histone modification processes. Recombinant DPY30 enables the dissection of its interactions with other proteins and nucleic acids, facilitating insights into its mechanistic pathways. Furthermore, elucidating the functional dynamics of DPY30 provides a foundation for developing targeted therapeutic strategies, particularly in malignancies associated with aberrant histone modifications. Overall, the study of DPY30 and its reconstituted forms is crucial for enhancing our understanding of epigenetic mechanisms and their implications for human health and disease.
