Analytical Data
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Gene name
Bcl3
- Application
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Alternative Names
Bcl3；BCL4；D19S37；B-cell lymphoma 3 Protein
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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
P20749
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Expression Region
全长
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AA Sequence
full
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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
Bcl-3 is a member of the Bcl-2 family of proteins, which play a crucial role in regulating apoptosis and cell survival. Unlike other Bcl-2 family members that primarily function as pro-apoptotic or anti-apoptotic factors, Bcl-3 is unique in its ability to function as a transcriptional regulator. It acts as an oncogenic factor by modulating the expression of genes involved in cell proliferation and survival, particularly in the context of various cancers. Research has demonstrated that Bcl-3 can interact with transcription factors, such as NF-κB, to enhance the expression of anti-apoptotic proteins, thereby promoting tumor growth and resistance to therapy. Given its significant role in cancer biology, the study of Bcl-3 has garnered considerable attention in the field of oncology. Recombinant Bcl-3 protein has been used in various studies to explore its biochemical properties, interactions with other proteins, and its influence on cellular processes. Furthermore, understanding the structural and functional aspects of Bcl-3 could provide insights into its potential as a therapeutic target for cancer treatments. The exploration of Bcl-3’s role in signaling pathways that lead to aberrant cell survival also holds promise for developing novel strategies to combat cancer and enhance the efficacy of existing therapies. As such, ongoing research into Bcl-3 and the implications of its dysregulation in cancer continues to be a dynamic and important area of interest in molecular biology and cancer therapeutics.
