CD40L (mouse) (multimeric) (rec.)
|Synonyms||MultimericCD40L™; ACRP30headless:CD40L; ACRP30headless:CD154; ACRP30headless:TNFSF5; ADIPOQ-CD40L|
|Sequence||Mouse CD40L (aa 115-260) is fused at the N-terminus to mouse ACRP30headless (aa 18-111) and a FLAG®-tag.|
|Specificity||Binds to human and mouse CD40.|
|Biological Activity||Induces B cells activation (as demonstrated by dose-dependent upregulation of CD86).|
|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.|
|Other Product Data||
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|
MultimericCD40L™ is a high activity construct in which two trimeric CD40 ligands are artificially linked via the collagen domain of ACRP30. This construct very effectively simulates the natural membrane-assisted aggregation of CD40L in vivo. It provides a simple and equally potent alternative to CD40L+enhancer combinations. MultimericCD40L™ has shown to suppress alum-induced IL-1β release and caspase-1 activation in a dose-, CD40- and time dependent manner, without affecting BMDM (Bone marrow-derived macrophages) viability. It also effectively suppressed the inflammasome function triggered by NLRP3 activators. The secretion of caspase-1 independent inflammatory mediators has been shown to be unaltered or even enhanced.
- Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex: N. Holler, et al.; Mol. Cell. Biol. 23, 1428 (2003)
- T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes: G. Guarda, et al.; Nature 460, 269 (2009)