Analytical Data
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Gene name
APRIL/TNFSF13 Trimer
- Application
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Alternative Names
CD256; TALL2; TALL-2; TNFSF13; APRIL; APRILFLJ57090; TRDL1; TRDL-1; ZTNF2; 2310026N09Rik
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Species
Human
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Source
HEK293
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Tag
N-Avi;N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75888-1
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Expression Region
Q111-L250
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Molecular Weight
55-63 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
Related Products
Protein Description
APRIL (A Proliferation-Inducing Ligand) and TNFSF13 (Tumor Necrosis Factor Superfamily Member 13) are key cytokines involved in the regulation of immune responses and B cell survival. APRIL functions as a trimeric protein that binds to its receptors, BAFF-R and TACI, influencing the proliferation, differentiation, and survival of B cells in the immune system. Due to its significant role in promoting B cell maturation and class switching, abnormalities in APRIL signaling are linked to various autoimmune diseases and malignancies. Research into recombinant forms of APRIL/TNFSF13 trimer proteins has gained traction as a potential therapeutic strategy, allowing for the detailed study of their mechanisms and effects on immune modulation. The availability of recombinant APRIL/TNFSF13 trims provides valuable tools for understanding the pathological processes involved in diseases characterized by dysregulated B cell activity. Furthermore, the trimeric structure is crucial for functional activity, as it enhances receptor binding and signaling efficacy. Through the investigation of this recombinant protein, researchers aim to uncover novel insights into the therapeutic targeting of B cell-related disorders and to develop innovative strategies for modulating immune responses in clinical settings. Overall, the study of APRIL/TNFSF13 trimer is at the forefront of immunological research, reflecting its potential applications in treating autoimmune diseases, lymphomas, and other immune-related conditions.
