Analytical Data
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Gene name
AQP1
- Application
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Alternative Names
Aquaporin-CHIP Urine water channel Water channel protein for red blood cells and kidney proximal tubule
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29972
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Expression Region
2-269aa
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Molecular Weight
29.9 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
BCL2 (B-cell lymphoma 2) is a crucial protein that plays a significant role in the regulation of apoptosis, or programmed cell death, which is essential for maintaining cellular homeostasis and preventing cancer development. Originally discovered in the context of B-cell lymphomas, the BCL2 gene is known to inhibit apoptosis, allowing for the survival of malignant cells and contributing to tumorigenesis. Given its pivotal role in cancer biology, BCL2 has become a prominent target for therapeutic intervention. Researchers have developed various BCL2 inhibitors to enhance the efficacy of existing cancer treatments and to overcome resistance to conventional therapies. The production of recombinant BCL2 protein has facilitated the study of its structure, function, and interactions with other apoptotic factors, thus advancing our understanding of its mechanisms in cellular survival and death. By using techniques such as molecular cloning and protein expression systems, scientists are able to produce BCL2 in sufficient quantities for biochemical assays and structural analyses. This research not only sheds light on the intricate balance between life and death in cells but also opens avenues for developing targeted therapies that could improve patient outcomes in cancers closely associated with BCL2 dysregulation. As the field progresses, the understanding of BCL2 and its related pathways continues to evolve, highlighting its importance in both basic research and clinical applications.
