BAFF/TNFSF13B Protein, Human (HEK293, Fc)

BAFF/TNFSF13B, is the B cell-activating cytokine belonging to the tumor necrosis factor family. BAFF is involved in cancer immunity and is mainly expressed in myeloid cells. Its overexpression can lead to autoimmune diseases such as systemic lupus erythematosus (SLE). In addition, BAFF is also involved in adipogenesis, atherosclerosis, neuroinflammatory process and ischemia/reperfusion (I/R) injury ^[1]. Human BAFF protein has two glycosylated domains and one transmembrane domain (48-68 a.a.), and can be cleaved into membrane-type peptide fragments and soluble peptide fragments. BAFF/TNFSF13B Protein, Human (HEK293, Fc) is the extracullar part of BAFF protein (A134-L285), produced in HEK293 cells with N-terminal hFc-tag.

B-cell Activating Factor (BAFF), belongs to tumor necrosis factor family, also known as B lymphocyte stimulator (BLyS), dendritic cell-derived TNF-like molecule, and TNF- and APOL-related leukocyte expressed ligand 1 (TALL-1). BAFF is the surpotor of autoreactive B cells, mainly expressed in myeloid cell lines. The expression level of BAFF is important with immunity, while excessive BAFF signaling can lead to autoimmunity. For example, BAFF is commonly overexpressed in Systemic Lupus Erythematosus (SLE). Furthermore, BAFF seems to be involved in adipogenesis, atherosclerosis, neuro-inflammatory processes and ischemia reperfusion (I/R) injury^[1]. DeltaBAFF is a conserved alternate splice isoform of BAFF, with a lack of 57 nt encoding the A-A1 loop. DeltaBAFF is co-expressed with BAFF in many mouse and human myeloid cells. DeltaBAFF in mouse is inefficiently released by proteolysis on plasma membrane, and binds to BAFF in heteromultimers to diminish BAFF bioactivity and release. Mouse BAFF protein has two glycosylated domains and one transmembrane domain (48-68 a.a.), and can be cleaved into membrane-type peptide fragments and soluble peptide fragments. Moreover, the protein sequences between human and mice are different with similarity of 68.23%^[2]. BAFF also involves in cancer immunity. BAFF upregulates multiple B cell costimulatory molecules; augments IL-12a expression and enhances B cell antigen-presentation to CD4⁺ Th cells in vitro. it also modulates T cell function through increased T cell activation and TH1 polarization, enhanced expression of the proinflammatory leukocyte trafficking chemokine CCR6, and promotion of a memory phenotype, leading to enhanced antitumor immunity. BAFF has distinct immunoregulatory functions, promoting the expansion of CD4+Foxp3+ Tregs in the spleen and tumor microenvironment (TME)^[3].

BAFF (human; 10 μg/kg; i.v.; single dose) resulted in a decrease in signaling through the non-canonical NF-κB pathway and a reduction in B-cells in the spleen in mice^[4].

Measured by its binding ability in a functional ELISA. When Recombinant BCMA Protein (HY-P70827) is immobilized at 2 µg/mL (100 µL/well) can bind Recombinant Human BAFF. The ED₅₀ for this effect is 9.159-13.72 ng/mL.

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  Measured by its binding ability in a functional ELISA. When Recombinant BCMA Protein(HY-P70827)is immobilized at 2 µg/mL (100 µL/well) can bind Recombinant Human BAFF. The ED₅₀ for this effect is 13.72 ng/mL.

Human

HEK293

N-hFc

Q9Y275-1 (A134-L285)

10673  [NCBI]

AVQGPEETVTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLL

Approximately 45-54.0 kDa due to the glycosylation.

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  Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4 or 20 mM Tris-HCl, 15%Trehalose, 4% Dextran-70, 0.05% Tween 80, pH 8.5 or PBS, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Möckel T, et al. B cell activating factor (BAFF): Structure, functions, autoimmunity and clinical implications in Systemic Lupus Erythematosus (SLE). Autoimmun Rev. 2021 Feb;20(2):102736.  [Content Brief]

  [2]. Gavin AL, et al. DeltaBAFF, an alternate splice isoform that regulates receptor binding and biopresentation of the B cell survival cytokine, BAFF. J Biol Chem. 2003 Oct 3;278(40):38220-8.  [Content Brief]

  [3]. Yarchoan M, et al. Effects of B cell-activating factor on tumor immunity. JCI Insight. 2020 May 21;5(10):e136417.  [Content Brief]

  [4]. Manetta J, et al. Generation and characterization of tabalumab, a human monoclonal antibody that neutralizes both soluble and membrane-bound B-cell activating factor. J Inflamm Res. 2014 Aug 20;7:121-31.  [Content Brief]