Analytical Data
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Gene name
E6
- Application
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Alternative Names
E6；9804；RIGE；SCA2；Lymphocyte antigen 6E
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Species
E.coli
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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
Q16553
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Expression Region
1-131aa
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AA Sequence
MKIFLPVLLAALLGVERASSLMCFSCLNQKSNLYCLKPTICSDQDNYCVTVSASAGIGNLVTFGHSLSKTCSPACPIPEGVNVGVASMGISCCQSFLCNFSAADGGLRASVTLLGAGLLLSLLPALLRFGP
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Molecular Weight
13.5 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
E6 recombinant protein has garnered significant attention in the field of cancer research, primarily due to its association with human papillomavirus (HPV) and its role in cervical cancer development. The E6 protein is known to interact with the host's tumor suppressor protein p53, leading to its degradation and disrupting the normal apoptosis pathway, ultimately contributing to uncontrolled cell proliferation. Understanding the molecular mechanisms by which E6 facilitates tumorigenesis is crucial for developing targeted therapies and vaccines against HPV-related cancers. Recent studies have focused on characterizing the structural and functional properties of E6, exploring its interactions with various cellular proteins, and identifying potential inhibitors that could mitigate its oncogenic effects. Additionally, the development of recombinant E6 proteins has provided insights into the protein's immunogenicity, paving the way for novel immunotherapeutic strategies. As researchers continue to unravel the complexities of E6 function and its role in the carcinogenic process, the findings hold promise for advancing prevention and treatment options for HPV-associated malignancies, thereby addressing a significant public health challenge.
