Analytical Data
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Gene name
BMF
- Application
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Alternative Names
BMF；Bcl-2-modifying factor
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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
Q96LC9
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Expression Region
1-184aa
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AA Sequence
MEPSQCVEELEDDVFQPEDGEPVTQPGSLLSADLFAQSLLDCPLSRLQLFPLTHCCGPGLRPTSQEDKATQTLSPASPSPGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAVLPIGEQPPEGQWQHQAEVQIARKLQCIADQFHRLHVQQHQQNQNRVWWQILLFLHNLALNGEENRNGAGPR
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Molecular Weight
47.5 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
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Protein Description
BMF (Bcl-2-modifying factor) is a pro-apoptotic protein that plays a significant role in regulating cell death and survival, particularly in the context of cancer. It functions by inhibiting the anti-apoptotic Bcl-2 family members, thus promoting apoptosis in cellular systems. The study of BMF and its recombinant protein form has gained importance due to its potential therapeutic implications in cancer treatment, considering that many cancers exploit the dysregulation of apoptotic pathways to evade cell death. Research has shown that BMF can sensitize cancer cells to chemotherapy by restoring the apoptotic response. Furthermore, variations in BMF expression levels have been implicated in various malignancies, linking its dysfunction to cancer progression and poor prognosis. The recombinant production of BMF allows for detailed studies on its structure-function relationships, interaction with other apoptotic proteins, and its role in cellular signaling pathways. This research is pivotal in developing novel cancer therapies targeted at modulating BMF activity, enhancing the efficacy of existing treatments, and ultimately improving patient outcomes. As such, understanding BMF at a molecular level could lead to breakthroughs in the design of strategies to manipulate apoptotic pathways in cancer therapy.
