APRIL (mouse) (H98) (multimeric) (rec.)
|Synonyms||MultimericAPRIL™; ACRP30headless:APRIL; ACRP30headless:CD256; ACRP30headless:TNFSF13; ACRP30headless:A-proliferation-inducing Ligand:|
The extracellular domain of mouse APRIL (aa 98-232) is fused at the N-terminus to mouse ACRP30headless (aa 18-110) and a FLAG®-tag.
Binds to human and mouse BCMA and TACI. Does not bind to proteoglycans.
Stimulates B cell proliferation.
|Endotoxin Content||<0.01EU/μg purified protein (LAL test; Lonza).|
|Concentration||0.1mg/ml after reconstitution.|
|Reconstitution||Reconstitute with 100μl sterile water.|
|Formulation||Lyophilized. Contains PBS + 0.5% Trehalose.|
|Other Product Data||
UniProt link Q9D777: APRIL (mouse)
FLAG is a registered trademark of Sigma-Aldrich Co.
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
After reconstitution, prepare aliquots and store at -20°C.
Avoid freeze/thaw cycles.
PBS containing at least 0.1% BSA should be used for further dilutions.
Stable for at least 6 months after receipt when stored at -20°C.
Working aliquots are stable for up to 3 months when stored at -20°C.
|Product Specification Sheet|
APRIL is a cytokine that belongs to the TNF superfamily and binds to TACI and BCMA. It is implicated in the regulation of tumor cell growth, is involved in monocyte/macrophage-mediated immunological processes and functions as an important survival factor for plasmablasts and bone marrow plasma cells. MultimericAPRIL™ is a high activity construct in which two trimeric APRIL ligands are artificially linked via the collagen domain of ACRP30. This construct very effectively stimulates proliferation B cell. A basic amino acid sequence (QKQKKQ) close to the NH2 terminus of APRIL is required for binding to negatively charged sulfated glycosaminoglycan side chains of proteoglycans. Proteoglycans mediate binding of APRIL to tumor cells as well as primary lymphoid cells.
- Selective APRIL blockade delays systemic lupus erythematosus in mouse: B. Huard, et al.; PLoS One 7, e31837 (2012)
- γ-secretase directly sheds the survival receptor BCMA from plasma cells: S.A. Laurent, et al.; Dissertation LMU (2015)