IL-5-1

E.coli

B-cell differentiation factor I, Eosinophil differentiation factor, TRF

Interleukin-5 (IL-5) is a secreted glycoprotein that belongs to the alpha -helical group of cytokines . Unlike other family members, it is present as a covalently linked antiparallel dimer. The cDNA for human IL-5 encodes a signal peptide and a 115 amino acid 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 crossreactivity 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 IL2stimulated invariant natural killer T cells (iNKT) . 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. 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 signaltransducing subunit, beta. IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed beta c dimers, forming a high-affinity receptor.

Approximately 26.5 kDa.

MIPTEIPTSA LVKETLALLS THRTLLIANE TLRIPVPVHK NHQLCTEEIF QGIGTLESQT VQGGTVERLF KNLSLIKKYI DGQKKKCGEE RRRVNQFLDY LQEFLGVMNT EWIIES

Sterile Filtered White lyophilized (freeze-dried) powder.

> 98% by SDS-PAGE and HPLC analyses.

Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

< 1.0 EU per 1μg of the protein

Lyophilized from a 0.2 µm filtered concentrated solution in 20mM PB, pH 7.5, 3% trehalose, 0.1% Tween-80.