Structural Formula Vector Image
Title: Interleukin-11
Additional Names: IL-11; adipogenesis inhibitory factor; AGIF
Literature References: Multifunctional cytokine produced by stromal cells such as fibroblasts, epithelial cells, and osteoblasts. Expressed in a wide variety of tissues, including CNS, thymus, lung, bone, and connective tissue. Nonglycosylated protein containing 178 amino acid residues; mol wt 19 kDa. Important regulator of hematopoiesis; stimulates growth of myeloid, erythroid, and megakaryocyte progenitor cells. Regulates bone metabolism; inhibits production of proinflammatory mediators; and protects against gastromucosal injury. Identification: S. R. Paul et al., Proc. Natl. Acad. Sci. USA 87, 7512 (1990). Identity with AGIF: I. Kawashima et al., FEBS Lett. 283, 199 (1991). Review of biological activity and clinical studies: X. Du, D. A. Williams, Blood 89, 3897-3908 (1997); A. J. Dorner et al., BioDrugs 8, 418-429 (1997). Review: P. F. Schendel, K. J. Turner in Cytokines, A. R. Mire-Sluis, R. Thorpe, Eds. (Academic Press, San Diego, 1998) pp 169-182.
Properties: Highly basic protein, pI 11.7. Rich in leucine (23%) and proline (12%). Has no disulfide bonds as it does not contain cysteine. Heat stable; melting temp 90°. Highly sol at physiologic pH.
Derivative Type: Oprelvekin
CAS Registry Number: 145941-26-0
CAS Name: 2-178-Interleukin 11 (human clone pXM/IL-11)
Trademarks: Neumega (Genetics Inst.)
Literature References: Human IL-11 produced in E. coli by recombinant DNA technology. Differs from naturally occurring protein only in the absence of the amino-terminal proline residue. Clinical pharmacokinetics: K. Aoyama et al., Br. J. Clin. Pharmacol. 43, 571 (1997). Clinical trial in chemotherapy-induced thrombocytopenia: I. Tepler et al., Blood 87, 3607 (1996); C. Isaacs et al., J. Clin. Oncol. 15, 3368 (1997). Review: J. A. Kaye, Curr. Opin. Hematol. 3, 209-215 (1996).
Therap-Cat: Hematopoietic.

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