Recombinant Human IL-11

Interleukin 11 (IL-11), also known as AGIF, is a member of the IL-6-type cytokine family and key regulator of multiple events in hemtaopoiesis. It stimulates growth of myeloid, erythroid and megakaryocyte progenitor cells.¹ IL-11 also regulates bone metabolism, inhibits production of proinflammatory cytokines and protects against gastromucosal injury.² Compared to other interleukins, IL-11 is relatively under-characterized. It is secreted by bone marrow stromal cells (fibroblasts) and is produced also by a number of mesenchymal cells. IL-11 is expressed in a wide variety of tissues including thymus, lung, bone, connective tissue and central nervous system. Signal transduction is initiated upon binding of IL-11 to IL-11Rα and gp130, facilitating the homodimerization of gp130 molecules.² This permits gp130-associated JAK kinases to become activated and phosphorylate intracellular tyrosine residues on gp130. IL-11 shares many functions of IL-6 and LIF, including potentiation of megakaryocyte activity, enhancement of human myeloma cell proliferation and enhancement of hepatic acute phase protein production.³ It has been found to stimulate the T cell dependent development of specific immunoglobulin-secreting B cells.⁴ Clinically, IL-11 is used to prevent severe thrombocytopenia and the reduction of the need for platelet transfusion following myelosuppressive chemotherapy. Another possible application may be as a therapeutic for osteoporosis.

The biological activity of Human IL-11 was determined by a cell proliferation assay using T11, a subline of the IL-6-dependent murine plasmacytoma cell line T1165.85.2.1 that has been adapted to grow in IL-11. (Nordan, R.P., Pumphrey, J.G., and B. Rudikoff, 1987, J. Immunol. 139:813). The expected ED₅₀ for this effect is typically 0.06 - 0.24 ng/ml.

pgpppgppr vspdpraeld stvlltrsll adtrqlaaql rdkfpadgdh nldslptlam sagalgalql pgvltrlrad llsylrhvqw lrraggsslk tlepelgtlq arldrllrrl qllmsrlalp qpppdppapp lappssawgg iraahailgg lhltldwavr gllllktrl

Pro22

Solution

The predicted molecular weight of Recombinant Human IL-11 is Mr 19 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 23 kDa.

19

This recombinant protein solution was 0.2 µm filtered and formulated in modified Dulbecco’s phosphate buffered saline (1X PBS) and 1mM EDTA, pH 7.2 – 7.4 with no calcium, magnesium, or preservatives present. The final protein concentration is 0.501 mg/ml.

Working aliquots of this recombinant protein solution are stable for up to six months at -20°C to -70°C in a manual defrost freezer. Upon thawing, in the presence of a carrier protein, this recombinant protein can be stored at 2° - 8°C for one month without detectable loss of activity. Product shows no detectable loss in activity after 3 months when aliquoted and stored at -20°C to -70°C in a manual defrost freezer. Avoid repeated freeze thaw cycles.

Next Day 2-8°C

1. Williams, DA. et al. (1990) Proc. Natl. Acad. Sci. (USA) 87:7512
2. Heinrich, PC. et al. (2003) Biochem. J. 374:1
3. Bauman, H. et al. (1991) J. Biol. Chem. 266:20424
4. Curti, A. et al. (2002) Haematologica 87:373