BAFF/TNFSF13B Protein, Mouse (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]. 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. BAFF/TNFSF13B Protein, Mouse (HEK293, Fc) is the extracullar part of BAFF protein (A127-L309), produced in HEK293 cells with N-terminal mFc-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 (5 μg/mL; 72 h) activated B cells demonstrate enhanced antigen-presentation (APC) to CD4+ Th cells in isolated CD4⁺ and CD8⁺ T cells^[3].
BAFF (5 μg/mL; 48 h) upregulates multiple B cell costimulatory molecules (CD21, CD23, CD40, CD5, CD80, CD86, ICOS-L, MHCII, and PD-L1) and induces a Be-1 phenotype in B cells^[3].

BAFF (mouse; 0.5 mg/kg; i.p.; daily for 7 d) upregulates B cell CD40 and PD-L1 expression in a syngeneic mouse model of melanoma, also increases T cell activation but also induces an increase in Treg frequency^[3].

Measured by its binding ability in a functional ELISA. When Recombinant Mouse BAFF Protein is immobilized at 2 µg/mL (100 µL/well) can bind Biotinylated Mouse BAFFR (HY-P7646). The ED₅₀ for this effect is < 3.0 ng/mL.

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  Measured by its binding ability in a functional ELISA. When Recombinant Mouse BAFF Protein is immobilized at 2 µg/mL (100 µL/well) can bind Biotinylated Mouse BAFFR (HY-P7646). The ED₅₀ for this effect is 2.991 ng/mL.

Mouse

HEK293

N-mFc

Q9WU72-1 (A127-L309)

24099  [NCBI]

Full Length of TNFSF13B soluble form

AFQGPEETEQDVDLSAPPAPCLPGCRHSQHDDNGMNLRNIIQDCLQLIADSDTPTIRKGTYTFVPWLLSFKRGNALEEKENKIVVRQTGYFFIYSQVLYTDPIFAMGHVIQRKKVHVFGDELSLVTLFRCIQNMPKTLPNNSCYSAGIARLEEGDEIQLAIPRENAQISRNGDDTFFGALKLL

Approximately 45-60 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

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  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 10% trehalose, 2% mannitol, 0.05% Tween 80, pH 8.0.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. 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]