BAFFR Human, HEK
HEK293 Cells.
Sterile Filtered colorless solution.
Greater than 95.0% as determined by SDS-PAGE.
Description
BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa.
BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Product Specs
Recombinant human BAFFR protein is a single, glycosylated polypeptide chain encompassing amino acids 1-78. It has a total of 314 amino acids, including a C-terminal fusion to a 233 amino acid hIgG tag, resulting in a molecular mass of 34.4 kDa. The protein is purified using proprietary chromatographic techniques.
Sterile filtered, colorless solution.
The BAFFR solution is provided at a concentration of 1 mg/ml in a buffer consisting of 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (up to 2-4 weeks), the BAFFR solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage to enhance protein stability. Repeated freeze-thaw cycles should be avoided to maintain protein integrity.
The purity of the BAFFR protein is greater than 95.0% as determined by SDS-PAGE analysis.
The protein's biological activity, measured as its effective concentration for 50% response (ED50) in a functional ELISA with human BAFF, is less than or equal to 0.7 µg/ml.
HEK293 Cells.
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.
Product Science Overview
B-cell activating factor (BAFF), also known as B-lymphocyte stimulator (BLyS), is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. It plays a crucial role in the development, proliferation, and differentiation of B cells. BAFF is expressed as a transmembrane protein on various cell types, including monocytes, dendritic cells, and bone marrow stromal cells .
BAFF contains a cytoplasmic domain, a transmembrane domain, and an extracellular domain. The extracellular domain can be cleaved to produce a soluble form detectable in serum . The recombinant form of BAFF, expressed in HEK 293 cells, is often used in research and therapeutic applications. This recombinant protein is typically lyophilized from a filtered solution and can be reconstituted in sterile PBS for use .
BAFF interacts with three primary receptors:
- BAFF-R (TNFRSF13C): This receptor is mainly expressed on mature B lymphocytes and is crucial for B cell survival and maturation.
- TACI (TNFRSF13B): Found on a subset of T cells and B cells, TACI has a higher affinity for a protein similar to BAFF called APRIL (A Proliferation-Inducing Ligand).
- BCMA (TNFRSF17): Expressed on plasma cells, BCMA can bind both BAFF and APRIL .
BAFF acts as a potent B cell activator and is essential for the proliferation and differentiation of B cells. It plays a significant role in the immune response by promoting B cell survival and immunoglobulin secretion. Elevated levels of BAFF are associated with various autoimmune diseases and hematological malignancies .
Due to its critical role in B cell regulation, BAFF has become a target for therapeutic interventions in diseases such as chronic lymphocytic leukemia (CLL) and multiple myeloma. Several BAFF-targeted therapies, including monoclonal antibodies like belimumab and atacicept, are being explored in clinical trials .
