Analytical Data
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Gene name
Bcl2
- Application
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Alternative Names
Bcl2；Apoptosis regulator Bcl-2
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Species
Human
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Source
E. coli
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Tag
C-terminal His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10415
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Expression Region
1-211aa
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AA Sequence
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPG HTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRY RRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESV NREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFD
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Molecular Weight
26.7kDa
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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
Identification
Protein Description
Bcl-2 (B-cell lymphoma 2) is a critical protein that plays a significant role in the regulation of apoptosis, or programmed cell death, which is essential for maintaining cellular homeostasis and tissue health. Originally discovered as an oncogene associated with certain types of lymphomas, Bcl-2 functions predominantly as an anti-apoptotic factor, protecting cells from the apoptotic process triggered by various stressors. Its dysregulation is linked to numerous cancers, making it a pivotal target for therapeutic interventions. The study of Bcl-2 recombinant proteins has gained traction in recent years, as these proteins can provide valuable insights into the mechanisms of apoptosis and cell survival. Researchers utilize recombinant DNA technology to produce Bcl-2 proteins, allowing for detailed structural and functional studies in different cellular environments. This research not only enhances our understanding of Bcl-2's role in cancer progression and resistance to therapies but also paves the way for developing novel treatments aimed at modulating its activity. The exploration of Bcl-2 protein interactions, its structural conformation, and its influence on mitochondrial dynamics further underscores the importance of this protein in both normal physiology and pathological conditions. Through these studies, scientists hope to uncover new avenues for targeted therapies, particularly in cancers where Bcl-2 is overexpressed, potentially leading to more effective treatments and improved patient outcomes.
