Analytical Data
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Gene name
TNFRSF3/LTBR
- Application
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Alternative Names
TNFCR; TNFR-RP; TNFR-III; TNFR2-RP; TNFRSF3; Tumor Necrosis Factor Superfamily Member 3; Tumor necrosis factor C receptor; Tumor necrosis factor receptor type III
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
P50284
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Expression Region
Pro128~Tyr395
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Molecular Weight
47kDa
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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
The study of TNFRSF3/LTBR (Tumor Necrosis Factor Receptor Superfamily Member 3/Lymphotoxin Beta Receptor) recombinant protein has gained significant attention in immunology and cancer research due to its crucial role in regulating immune responses and its involvement in lymphoid organ development. LTBR is primarily expressed on lymphoid tissues and various immune cells, influencing lymphocyte proliferation, survival, and differentiation. Additionally, LTBR signaling is essential for maintaining the architecture of secondary lymphoid organs and facilitating the interaction between different immune cell types. Dysregulation of this pathway is implicated in various disease states, including autoimmune disorders and cancer. The production of recombinant LTBR protein enables detailed studies of its structure-function relationships and the exploration of its potential as a therapeutic target. By utilizing recombinant technologies, researchers can investigate how LTBR signaling pathways can be modulated to enhance anti-tumor immunity or suppress inappropriate inflammatory responses. Moreover, understanding the biomechanical interactions between LTBR and its ligands may lead to innovative strategies for augmenting immune responses in clinical applications, such as cancer immunotherapy. Overall, the exploration of TNFRSF3/LTBR recombinant protein represents a promising avenue for advancing our knowledge of immune regulation and developing new therapeutic approaches against diseases characterized by immune dysfunction.
