Analytical Data
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Gene name
SETD7
- Application
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Alternative Names
SETD7;KIAA1717;KMT7;SET7;Histone-lysine N-methyltransferase SETD7
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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
Q8WTS6
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Expression Region
1-366aa
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AA Sequence
MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGK FFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDT DGRLIFKGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPD ERTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSC ISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRI THQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFT PNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAP EWYQVELKAFQATQQK
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Molecular Weight
75 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
SETD7, a lysine methyltransferase, plays a crucial role in epigenetic regulation by catalyzing the methylation of lysine 4 on histone H3 (H3K4), which is associated with transcriptional activation. This enzyme has garnered significant interest due to its involvement in various cellular processes, including gene expression, DNA damage response, and cell differentiation. Abnormal SETD7 activity has been linked to several diseases, including cancer, where it may influence tumor progression and metastasis. Researchers are particularly interested in SETD7's potential as a therapeutic target, as inhibiting its activity may disrupt pathways that contribute to malignancy. Furthermore, the study of recombinant SETD7 proteins allows for a better understanding of its structural and functional properties, aiding in the development of small-molecule inhibitors and elucidating its role in disease mechanisms. The ability to express SETD7 in a purified form facilitates biochemical assays and structural biology studies, providing insights into its interaction with substrates and other regulatory proteins within the epigenetic landscape. Thus, ongoing research on SETD7 recombinant proteins is vital for advancing our knowledge in epigenetics and cancer biology, paving the way for novel therapeutic approaches leveraging SETD7 modulation.
