The recombinant human TNFRSF13C protein (BAFF receptor) is a truncated, bioactive form of the tumor necrosis factor receptor superfamily member 13C. This partial protein (typically spanning amino acids 7–71) is engineered for research applications to study BAFF-mediated signaling, B-cell development, and immune regulation. It is produced in mammalian or bacterial expression systems and retains functional binding activity with BAFF (TNFSF13B). Key applications include investigating autoimmune diseases, B-cell malignancies, and immunodeficiency disorders .
Recombinant TNFRSF13C is synthesized using plasmid constructs encoding specific amino acid regions (e.g., 7–71) and expressed in:
Host System | Tag | Purity | Endotoxin Level | Source |
---|---|---|---|---|
HEK-293 cells | His, Fc, or Avi | >95% (SDS-PAGE) | <1.0 EU/μg | |
E. coli | None | >95% (SDS-PAGE) | <1.0 EU/μg |
Tags: Fc, His, or Avi tags enhance solubility and purification.
Activity Validation: ELISA confirms binding to BAFF with EC₅₀ values of 9.943–15.72 ng/ml (unlabeled BAFF) and 0.2699–0.5613 ng/ml (biotinylated BAFF) .
Assay Type | Target | EC₅₀ | Application | Source |
---|---|---|---|---|
ELISA | TNFSF13B | 0.27–15.7 ng/ml | BAFF-R interaction specificity | |
Splenocyte Survival | BAFF-induced B-cell survival | 1.0–5.0 μg/ml | In vitro B-cell survival studies |
Mechanism: BAFF-R binds BAFF via its extracellular domain, activating NF-κB and MAPK pathways to promote B-cell maturation and survival .
Common Variable Immunodeficiency (CVID): Mutations in TNFRSF13C (e.g., del89–96) impair BAFF-R expression, leading to reduced transitional B-cell maturation and hypogammaglobulinemia .
Systemic Lupus Erythematosus (SLE): Elevated BAFF levels correlate with autoreactive B-cell survival .
Lymphomas: BAFF-R is overexpressed in follicular lymphoma and mantle cell lymphoma, making it a therapeutic target .
Antibody Development: Humanized anti-BAFF-R antibodies (e.g., afucosylated variants) show efficacy in preclinical models of B-cell cancers .
Variant | Effect | Disease Association | Source |
---|---|---|---|
H159Y | Altered BAFF binding | Severe COVID-19 susceptibility | |
del89–96 | Transmembrane domain truncation | CVID-like immunodeficiency |
Clinical Relevance: BAFF-R deficiency results in:
Parameter | HEK-293-Expressed (7–71 aa) | E. coli-Expressed (7–76 aa) | Fc-Chimera |
---|---|---|---|
Purity | >95% | >90% | >95% |
Endotoxin | <1.0 EU/μg | <1.0 EU/μg | <1.0 EU/μg |
Tag | His, Fc | None | Fc |
Activity | BAFF binding (EC₅₀: 0.27–15.7 ng/ml) | BAFF binding (EC₅₀: N/A) | BAFF blocking (ED₅₀: 20–80 ng/ml) |
This Recombinant Human TNFRSF13C (CD268) protein is a valuable tool for cancer research. TNFRSF13C, also known as Tumor necrosis factor receptor superfamily member 13C, plays a critical role in immune regulation and is implicated in various cancer-related processes.
Our TNFRSF13C protein is produced using an E. coli expression system and encompasses amino acids 1 to 76, representing a partial length of the TNFRSF13C sequence. It is tag-free, ensuring its native conformation and eliminating any potential interference in downstream applications. With a purity exceeding 95% and minimal endotoxin contamination, our TNFRSF13C protein provides reliable and consistent results.