United States (US)

IL15 protein

Cat No. GTX29583

Reactivity Human
Species Human


Lyophilized powder


Lyophilized from 20mM Tris, pH 8.0.


The lyophilized protein is stable for a few weeks at room temperature, but best stored at -20 ºC. We recommend a quick spin followed by reconstitution in water to a concentration of 0.1-1.0mg/ml. This solution can then be diluted into other aqueous b

Antigen Species



Highly pure (>98%) recombinant hIL-11 (human Interleukin-11)


Highly pure (>98%) recombinant hIL-11 (human Interleukin-11)


Sterile filtered Greater than 98% pure by SDS-PAGE and HPLC analyses. Endotoxin level is less than 0.1 ng per μg (1EU/μg).


For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.


Interleukin 15,Il-15,Il15

Cellular Localization



IL15 (114 amino acids) has a predicted molecular mass of approximately 12.5 kDa. Human IL15 shares approximately 97% and 73% amino acid sequence identity with simian and mouse IL15, respectively. Both human and simian IL15 are active on mouse cells. IL15 was initially isolated from the simian kidney epithelial cell line CV1/EBNA. It has also been isolated from mouse and human cell sources. The cytokines IL15 and IL2 share many biological properties and stimulatory activities (T, B, and NK cells). Both IL15 and IL2 stimulate mouse CTLL2 cells. In activated peripheral blood T lymphocytes, IL2 is highly expressed but the expression of IL15 is not detectable. There is no sequence homology between IL15 and IL2, though computer modeling indicates both possess a four alpha-helical bundle structure. IL15 competes for binding sites with IL2, as both IL2 and IL15 stimulate the growth of cells through the IL2 receptor. IL15 mRNA is expressed in many cell types and tissues including adherent peripheral blood mononuclear cells, fibroblasts, and epithelial cells, monocytes, placenta, and skeletal muscle.

Research Area