Analytical Data
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Gene name
Bcl-2-like 蛋白 11
- Application
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Alternative Names
Bcl2-interacting mediator of cell death
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43521
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Expression Region
1-198aa
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Molecular Weight
38.2 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
Bcl-2-like protein 11 (Bcl-2L11), also known as Bok, is a member of the Bcl-2 family of proteins, which play critical roles in the regulation of apoptosis, or programmed cell death. This family is divided into pro-apoptotic and anti-apoptotic members, and Bcl-2L11 is primarily characterized as a pro-apoptotic factor. Research has shown that Bcl-2L11 is involved in various cellular processes, including apoptosis, cell cycle regulation, and response to stress. Its expression is often tightly regulated, and dysregulation can lead to various pathological conditions, including cancer, where the evasion of apoptosis is a hallmark of tumor progression. Recombinant Bcl-2L11 protein has gained attention in scientific research due to its potential therapeutic applications and its roles in understanding apoptosis mechanisms. Studies have focused on the structural characterization, functional analysis, and interactions of Bcl-2L11 with other proteins to elucidate its precise role in apoptosis signaling pathways. Moreover, the recombinant form of this protein can be useful in drug discovery and development, particularly in creating new cancer therapies that aim to restore apoptotic pathways in malignant cells. Understanding Bcl-2L11’s functions and mechanisms through recombinant protein research could provide significant insights into cancer biology and lead to innovative strategies for cancer treatment.
