Cat. #:101-15
Recombinant Human Interleukin-15
Technical Parameters
Source Escherichia coli.
Molecular Weight Approximately 12.9 kDa, a single non-glycosylated polypeptide chain containing 114 amino acids.
Quantity 2µg/10µg/1000µg
Purity > 97 % by SDS-PAGE and HPLC analyses.
Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Endotoxin Less than 1 EU/µg of rHuIL-15 as determined by LAL method.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Usage This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.
Reference1. Anderson DM, Johnson L, Glaccum MB, et al. 1995. Genomics, 25: 701-6.
2. Krause H, Jandrig B, Wernicke C, et al. 1996. Cytokine, 8: 667-74.
3. Chirifu M, Hayashi C, Nakamura T, et al. 2007. Nat Immunol, 8: 1001-7.
4. Grabstein KH, Eisenman J, Shanebeck K, et al. 1994. Science, 264: 965-8.
5. Giri JG, Ahdieh M, Eisenman J, et al. 1994. EMBO J, 13: 2822-30.
6. Arena A, Merendino RA, Bonina L, et al. 2000. New Microbiol, 23: 105-12.
BackgroundHuman Interleukin-15 (IL-15) is expressed by the IL15 gene located on the chromosome 4. It shares approximately 97 % and 73 % sequence identity with simian and murine IL-15, respectively. Both human and simian IL-15 are active on murine cells. IL-15 is secreted by mononuclear phagocytes (and some other cells), especially macrophages following infection by virus. It possesses a variety of biological functions, including stimulating and maintaining of cellular immune responses, especially regulating T and natural killer (NK) cell activation and proliferation. In additionally, it shares many biological properties with IL-2, including T, B and NK cell-stimulatory activities. IL-15 signals through a complex composed of IL-2/IL-15 receptor beta chain. Although IL-15 lacks sequence homology with IL-2, it has recently been shown that both the beta and gamma chains of the IL-2 receptor are utilized for IL-15 binding and signaling. In addition, an IL-15 specific binding protein has also been cloned from a mouse T cell clone.