Analytical Data
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Gene name
SET
- Application
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Alternative Names
SET;Protein SET
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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
Q01105
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Expression Region
1-290aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPKRQS PLPPQKKKPR PPPALGPEET SASAGLPKKG EKEQQEAIEH IDEVQNEIDR LNEQASEEIL KVEQKYNKLR QPFFQKRSEL IAKIPNFWVT TFVNHPQVSA LLGEEDEEAL HYLTRVEVTE FEDIKSGYRI DFYFDENPYF ENKVLSKEFH LNESGDPSSK STEIKWKSGK DLTKRSSQTQ NKASRKRQHE EPESFFTWFT DHSDAGADEL GEVIKDDIWP NPLQYYLVPD MDDEEGEGEE DDDDDEEEEG LEDIDEEGDE DEGEEDEDDD EGEEGEEDEG EDD
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Molecular Weight
36 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
SET (also known as SET nuclear oncogene) is a multifunctional protein that plays a significant role in various cellular processes, including transcriptional regulation, apoptosis, and DNA repair. Its involvement in cancer has garnered considerable attention, as SET has been implicated in the progression and development of several malignancies. Research has shown that SET interacts with various proteins, such as histone methyltransferases and transcription factors, influencing gene expression and cellular responses to stress. Moreover, SET acts as a negative regulator of the apoptotic process, allowing cancer cells to evade programmed cell death, which is a hallmark of tumorigenesis. Given its central role in these critical biological pathways, SET has emerged as a potential therapeutic target for cancer treatment. Recent studies focus on elucidating the precise mechanisms by which SET functions, including its post-translational modifications and interactions with other signaling molecules in the tumor microenvironment. Understanding the structure and function of SET, as well as its reorganization in pathological conditions, could pave the way for novel strategies in cancer therapy, offering hope for improved treatment outcomes in patients with SET-related malignancies.
