Analytical Data
-
Gene name
TNFRSF13B
- Application
-
Alternative Names
TNFRSF13B;TACI;Tumor necrosis factor receptor superfamily member 13B
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O14836
-
Expression Region
2-120aa
-
AA Sequence
SGLGRSRRGGRSRVDQEERFPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCRSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLRSPVNLPPELRR
-
Molecular Weight
14.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
TNFRSF13B, also known as TACI (Transmembrane Activator and CAML Interactor), is a member of the tumor necrosis factor receptor superfamily that plays a crucial role in the immune response, particularly in B cell regulation and class-switch recombination. Dysregulation of TNFRSF13B is associated with various autoimmune diseases and immunodeficiencies, including common variable immunodeficiency (CVID). Research on recombinant TNFRSF13B protein aims to elucidate its structure-function relationship and its role in signaling pathways involved in B cell activation and survival. Understanding TNFRSF13B’s mechanisms can provide insights into its contribution to pathophysiological conditions and open avenues for therapeutic interventions. For instance, recombinant forms of TNFRSF13B can be used in experimental models to assess their effects on immune cell behavior and to screen for potential pharmacological agents. Furthermore, investigations into the protein's interactions with ligands and downstream signaling components can enhance our comprehension of the immune system's complexity. Advances in recombinant protein technology have facilitated the production of this biomolecule, allowing for detailed biochemical characterization and functional assays, which are essential for exploring therapeutic applications targeting TNFRSF13B-related disorders. Thus, ongoing research endeavors are crucial for unraveling the implications of TNFRSF13B in health and disease.











