Recombinant Mouse BAFF (carrier-free)

Pricing & Availability
Other Names
B cell activating factor belonging to the TNF family (BAFF), B lymphocytes stimulator (BLyS), TNF- and APOL-related leukocyte expressed ligand 1 (TALL1), TNF homolog that activates apoptosis, NKFB, and JNK (THANK), Tnfsf13b, CD257
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Product Citations
publications
BAFF_Mouse_Recombinant_Protein_BA_100213
B cell proliferation induced by mouse BAFF.
  • BAFF_Mouse_Recombinant_Protein_BA_100213
    B cell proliferation induced by mouse BAFF.
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591202 10 µg 304€
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Description

BAFF is a TNF cytokine member (a type II membrane protein) that acts in both a membrane-bound form and soluble cytokine form. The extracellular domain of BAFF shows high homology with APRIL. The soluble form is derived by a cleavage in a furin consensus site. In human neutrophils treated with G-CSF, BAFF is processed intracellularly by a furin-type convertase. BAFF acts mainly as a soluble trimer and binds to three receptors, with decreasing affinity in the following order: BAFFR > TACI > BCMA. Mice deficient in BAFF or its receptor BAFFR exhibit an obstruction in B cell development after the transitional T1 stage and lack a marginal zone (MZ) and conventional B2 B cells. BAFFR-deficient mice and humans (patients with common variable immunodeficiency, CVID) develop severe B cell lymphopenia due to the arrest of B cell development at the transitional B cell stage. Extreme BAFF production triggers severe autoimmune disorders in mice similar to systemic lupus erythematosus and Sjögren’s syndrome. BAFF has been associated with different human diseases such as pancreatic ductal adenocarcinoma (PDAC), autoimmune pancreatitis, systemic lupus erythematosus, rheumatoid arthritis, Sjögren's syndrome, lymphoid cancers, HIV infection, and B cell malignancies such as non-Hodgkin's lymphoma (NHL).

Product Details
Technical Data Sheet (pdf)

Product Details

Reactivity
Mouse
Source
Mouse BAFF, amino acids Ala127-Leu309 (Accession# NM_033622) was expressed in CHO cells.
Molecular Mass
The 204 amino acid recombinant protein has a predicted molecular mass of approximately 22.8 kD. The DTT-reduced and non-reduced protein migrate at approximately 20-25 and 50-55 kD by SDS-PAGE respectively. The N-terminal contains a 9His-2(SGGG)-IEGR-tag.
Purity
>95%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS pH 6.5.
Endotoxin Level
Less than 1 EU per µg cytokine as determined by the LAL method.
Concentration
10 µg size is bottled at 50 µg/mL.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 µg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1% BSA or HSA. After dilution, the cytokine can be stored between 2°C and 8°C for one month or from -20°C to -70°C for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
ED50 = 0.5 - 3 ng/ml, corresponding to a specific activity of 0.33 - 2.0 x 106 units/mg, as determined by the dose dependent stimulation of B cells proliferation.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are validated in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Product Citations
  1. Han S, et al. 2016. Arthritis Res Ther. 0.975. PubMed
  2. Hennenberg E, et al. 2017. PLoS One. 10.1371/journal.pone.0180834. PubMed
  3. Vicioso Y, et al. 2019. Cancer Immunol Res. 7:1106. PubMed
Publication Library

Antigen Details

Distribution
Monocytes, macrophages, dendritic cells, neutrophils, and stromal cells of lymphoid organs.
Function
BAFF induces B cell maturation, proliferation, survival, and immunoglobulin production. BAFF controls the size and composition of mature preimmune B cell pools. BAFF is induced by INFγ in monocytes.
Interaction
Immature B cells, peripheral B-cells, naïve and memory cells.
Ligand/Receptor
BAFFR, TACI (transmembrane activator and calcium-modulator and cyclophilin ligand interactor), and BCMA (B cell maturation antigen).
Cell Type
Embryonic Stem Cells
Biology Area
Cell Biology, Signal Transduction, Stem Cells, Immunology, Costimulatory Molecules
Molecular Family
Growth Factors, Cytokines/Chemokines, Soluble Receptors, CD Molecules
Antigen References

1. Schneider P, et al. 1999. J. Exp. Med. 189:1747.
2. Nardelli B, et al. 2001. Blood 97:198.
3. Schiemann S, 2001. Sciences 293:2111.
4. Scapini P, et al. 2003. J. Exp. Med. 197:297.
5. Yeramilli VA and Knight KL. 2010. J. Immunol. 184:5527.
6. Scholz JL and Cancro MP. 2012. Immunol. Lett. 143:2.
7. Sindhava VJ, et al. 2013. Front. Immunol. 4:37.
8. Koizumi M, et al. 2013. PLoS One 8:e71367.

Gene ID
24099 View all products for this Gene ID
UniProt
View information about BAFF on UniProt.org

Related FAQs

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

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For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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