17.0 kD (Reducing)
Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
William Cruikshank. Crit Rev Immunol. 2008;28(6):467-83.
Intcrleukin-16 (IL-16) was originally identified in 1980 as the first-described T-cell chemoattractant. Since that time, the protein has been cloned, sequenced, and characterized in terms of expression and biologic function for regulating inflammation. Generated as a precursor molecule, IL-16 is cleaved by caspase-3, yielding pro-IL-16 and the secreted (mature) portion. Both components of IL-16 are now known to regulate T-cell growth and represent one of the few proteins for which function has been determined for both the pro- and secreted portions. Secreted IL-16 primes CD4+ T cells for IL-2 and IL-15 responsiveness, with a preferential effect on TH1 cells. Animal models have identified its involvement in the establishment of TH1-type inflammation with a critical role in the development of certain autoimmune diseases. Nuclear pro-IL-16 is a recently identified regulator of Skp2 transcription and T- cell cycle progression, acting as a scaffold protein for GABPbeta and histone deacctylase-3.
1μg (R: reducing condition, N: non-reducing condition).
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-16 is immobilized 5µg/mL (100 µl/well), Recombinant Human CD4/LEU3 His binds with an EC50 of 0.17-0.31μg/ml.
您现在的位置：
