IL-15 Protein
-
- Target See all IL-15 (IL15) Proteins
- IL-15 (IL15) (Interleukin 15 (IL15))
- Protein Type
- Recombinant
- Biological Activity
- Active
-
Origin
- Human
-
Source
- Escherichia coli (E. coli)
- Sequence
- MNWVNVISDL KKIEDLIQSM HIDATLYTES DVHPSCKVTA MKCFLLELQV ISLESGDASI HDTVENLIIL ANNSLSSNGN VTESGCKECE ELEEKNIKEF LQSFVHIVQM FINTS
- Purity
- > 96 % by SDS-PAGE and HPLC analyses.
- Sterility
- 0.2 μm filtered
- Endotoxin Level
- Less than 1EU/µg of rHuIL-15 as determined by LAL method.
- Top Product
- Discover our top product IL15 Protein
-
-
- Restrictions
- For Research Use only
-
- Format
- Lyophilized
- 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.
- Storage
- 4 °C/-20 °C
-
- Target
- IL-15 (IL15) (Interleukin 15 (IL15))
- Alternative Name
- IL-15 (IL15 Products)
- Synonyms
- IL15 Protein, AI503618 Protein, IL-15 Protein, interleukin 15 Protein, IL15 Protein, Il15 Protein
- Background
- Interleukin 15 is a recently identified novel cytokine that shares many biological properties with IL-2, including T, B and NK cell-stimulatory activities. cDNA clones encoding this cytokine have been isolated from simian, murine and human cell sources. Human IL-15 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. Human IL-15 cDNA encodes a 162 amino acid residue precursor protein containing a 48 amino acid residue signal peptide that is cleaved to yield the 114 amino acid residue mature protein. The IL-15 mRNA is expressed by a wide variety of cells and tissues and is most abundantly expressed by adherent peripheral blood mononuclear cells, fibroblasts and epithelial cells. However, in activated peripheral blood T lymphocytes where IL-2 is highly expressed, the expression of IL-15 is not detectable. 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. (Grabstein, K. et al., 1994, Science 264:965, Giri, J. et al., 1994, EMBO J. 13:2822).
- Pathways
- JAK-STAT Signaling, Glycosaminoglycan Metabolic Process
-