1 μg/lane of Recombinant Human IL-5 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 13-15 kDa and 28-32 kDa, respectively.
Recombinant Human IL-5 (Catalog # 205-IL) stimulates cell proliferation of the TF-1 human erythroleukemic cell line. The ED50 for this effect is 0.04-0.2 ng/mL.
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.01 EU per 1 μg of the protein by the LAL method.
13 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Interleukin-5 (IL-5) is a secreted glycoprotein that belongs to the alpha -helical group of cytokines (1 ‑ 3). Unlike other family members, it is present as a covalently linked antiparallel dimer (4, 5). The cDNA for human IL-5 encodes a signal peptide and a 115 amino acid (aa) mature protein. Mature human IL-5 shares 70%, 70%, 62%, 71%, 70% and 66%, aa sequence identity with mouse, rat, canine, equine, feline and porcine IL-5, respectively and shows cross‑reactivity with mouse IL-5. IL-5 is primarily produced by CD4+ Th2 cells, but also by activated eosinophils, mast cells, EBV-transformed B cells, Reed-Sternberg cells in Hodgkin’s disease, and IL‑2‑stimulated invariant natural killer T cells (iNKT) (1 ‑ 3, 6 ‑ 8). IL-5 increases production and mobilization of eosinophils and CD34+ progenitors from the bone marrow and causes maturation of eosinophil precursors outside the bone marrow (1, 6, 9, 10). The receptor for human IL-5, mainly expressed by eosinophils, but also found on basophils and mast cells, consists of a unique ligand-binding subunit (IL-5 R alpha ) and a shared signal‑transducing subunit, beta c (3, 6, 11). IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed beta c dimers, forming a high-affinity receptor (12). IL-5 also binds proteoglycans, potentially enhancing its activity (13). Soluble forms of IL-5 R alpha antagonize IL-5 and can be found in vivo (10, 14). In humans, IL-5 primarily affects cells of the eosinophilic lineage, and promotes their differentiation, maturation, activation, migration and survival, while in mice IL-5 also enhances Ig class switching and release from B1 cells (1 ‑ 3, 9, 10, 15, 16). IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release (17).
Rosenberg, H. F. et al. (2007) J. Allergy Clin. Immunol. 119:1303.
Elsas, P.X. and M. I. G. Elsas (2007) Curr. Med. Chem. 14:1925.
Martinez-Moczygemba, M. and D. P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
Minamitake, Y. et al. (1990) J. Biochem. 107:292.
McKenzie, A. N. et al. (1991) Mol. Immunol. 28:155.
Shakoory, B. et al. (2004) J. Interferon Cytokine Res. 24:271.
Lalani, T. et al. (1999) Ann. Allergy Asthma Immunol. 82:317.
Sakuishi, K. et al. (2007) J. Immunol. 179:3452.
Clutterbuck, E. J. et al. (1989) Blood 73:1504.
Cameron, L. et al. (2000) J. Immunol. 164:1538.
Tavernier, J. et al. (1991) Cell 66:1175.
Zaks-Zilberman, M. et al. (2008) J. Biol. Chem. 283:13398.
Lipscombe, R. et al. (1998) J. Leukocyte Biol. 63:342.
Tavernier, J. et al. (2000) Blood 95:1600.
Kopf, M. et al. (1996) Immunity 4:15.
Horikawa, K. and K. Takatsu (2006) Immunology 118:497.
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.
Review this Product
Be the first to review our Recombinant Human IL-5 Protein and receive a gift card or discount.