|Molecular Weight||Approximately 12.9 kDa, a single non-glycosylated polypeptide chain containing 114 amino acids.|
|AA Sequence||NWVNVISDLK KIEDLIQSMH IDATLYTESD VHPSCKVTAM KCFLLELQVI SLESGDASIH DTVENLIILA NNSLSSNGNV TESGCKECEE LEEKNIKEFL QSFVHIVQMF INTS|
|Purity||> 98 % 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 0.01 EU/µg of rHuIL-15 GMP 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 GMP product can be for research use or further manufacturing use.|
|Quality statement||The manufacture and testing of this product is in compliance with ICH Q7a guidelines.|
|Reference||1. 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.
|Background||Human 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.|