Recombinant Equine IL-5 Protein, CF

• Reactivity: Eq
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Equine IL-5 Protein, CF Summary

• Details of Functionality: Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED 50 for this effect is 4-16 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived equine IL-5 protein Leu20-Gly134, with a C-terminal 6-His tag
• Accession #: O02699
• N-terminal Sequence: Leu20
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 13.9 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.
• SDS-PAGE: 19 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Equine IL-5 Protein, CF

• BCDF mu
• B-cell differentiation factor I
• BCGFII
• EDF
• Eo-CSF
• Eosinophil differentiation factor
• IL5
• IL-5
• IL-5T-cell replacing factor
• interleukin 5 (colony-stimulating factor, eosinophil)
• interleukin-5
• TRF
• TRFB cell differentiation factor I

Background

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). Equine IL-5 is synthesized as a 134 amino acid (aa) precursor that contains a 19 aa signal sequence and a 115 aa mature segment. Mature equine IL-5 shares 71%, 66%, 63%, 83%, 88% and 85%, aa sequence identity with human, mouse, rat, canine, feline and porcine IL-5, respectively. 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).

1. Rosenberg, H. F. et al. (2007) J. Allergy Clin. Immunol. 119:1303.
2. Elsas, P.X. and M. I. G. Elsas (2007) Curr. Med. Chem. 14:1925.
3. Martinez-Moczygemba, M. and D. P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
4. Minamitake, Y. et al. (1990) J. Biochem. 107:292.
5. McKenzie, A. N. et al. (1991) Mol. Immunol. 28:155.
6. Shakoory, B. et al. (2004) J. Interferon Cytokine Res. 24:271.
7. Lalani, T. et al. (1999) Ann. Allergy Asthma Immunol. 82:317.
8. Sakuishi, K. et al. (2007) J. Immunol. 179:3452.
9. Clutterbuck, E. J. et al. (1989) Blood 73:1504.
10. Cameron, L. et al. (2000) J. Immunol. 164:1538.
11. Tavernier, J. et al. (1991) Cell 66:1175.
12. Zaks-Zilberman, M. et al. (2008) J. Biol. Chem. 283:13398.
13. Lipscombe, R. et al. (1998) J. Leukocyte Biol. 63:342.
14. Tavernier, J. et al. (2000) Blood 95:1600.
15. Kopf, M. et al. (1996) Immunity 4:15.
16. Horikawa, K. and K. Takatsu (2006) Immunology 118:497.
17. Denburg, J. A. et al. (1991) Blood 77:1462.

Bioinformatics

• Uniprot:
  • O02699()