Recombinant Cotton Rat IL-13 Protein

• Reactivity: Cr
• Applications: Bioactivity

Recombinant Cotton Rat IL-13 Protein 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 3 - 18 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived cotton rat IL-13 protein Met1-His133, with a C-terminal 5-His tag
• Accession #: AAP93198
• N-terminal Sequence: Gly21
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 13.1 kDa.
  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: 15-30 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 with BSA as a carrier protein.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Cotton Rat IL-13 Protein

• ALRHMGC116789
• BHR1interleukin-13
• IL13
• IL-13
• IL-13MGC116788
• interleukin 13
• MGC116786
• NC30
• P600

Background

IL-13 is a 17 kDa immunoregulatory cytokine that plays a key role in the pathogenesis of allergic asthma and atopy. It is secreted by Th1 and Th2 CD4 + T cells, NK cells, visceral smooth muscle cells, eosinophils, mast cells, and basophils (1 - 4). IL-13 circulates as a monomer with two internal disulfide bonds that contribute to a bundled four alpha -helix configuration (5, 6). Mature cotton rat IL-13 shares 59%, 74%, and 72% amino acid sequence identity with human, mouse, and rat IL-13, respectively. Despite the low homology, it exhibits cross-species activity between human, mouse, and rat (7, 8). IL-13 has diverse activities on numerous cell types (9). On macrophages, IL-13 suppresses the production of proinflammatory cytokines and other cytotoxic substances. On B cells, IL-13 induces immunoglobulin class switching to IgE, up-regulates the expression of MHC class II, CD71, CD72, and CD23, and costimulates proliferation. IL-13 up-regulates IL-6 while down-regulating IL-1 and TNF-alpha production by fibroblasts and endothelial cells. IL-13 binds with low affinity to IL-13 R alpha 1, triggering IL-13 R alpha 1 association with IL-4 R alpha . This high affinity receptor complex also functions as the type 2 IL-4 receptor complex (10, 11). Additionally, IL-13 binds with high affinity to IL-13 R alpha 2 which is expressed intracellularly, on the cell surface, and as a soluble molecule (12 - 15). IL-13 R alpha 2 regulates the bioavailability of both IL-13 and IL-4 and is overexpressed in glioma and several bronchial pathologies (11, 16, 17). Compared to wild type IL-13, the atopy-associated R110Q variant of IL-13 elicits increased responsiveness from eosinophils that express low levels of IL-13 R alpha 2 (18).

1. Wills-Karp, M. (2004) Immunol. Rev. 202:175.
2. Nakajima H. and K. Takatsu (2007) Int. Arch. Allergy Immunol. 142:265.
3. McKenzie, A.N. et al. (1993) Proc. Natl. Acad. Sci. 90:3735.
4. Blanco, J.C.G. et al. (2004) J. Interferon Cytokine Res. 24:21.
5. Moy, F.J. et al. (2001) J. Mol. Biol. 310:219.
6. Eisenmesser, E.Z. et al. (2001) J. Mol. Biol. 310:231.
7. Ruetten, H. and C. Thiemermann (1997) Shock 8:409.
8. Lakkis, F.G. et al. (1997) Biochem. Biophys. Res. Commun. 235:529.
9. Wynn, T.A. (2003) Annu. Rev. Immunol. 21:425.
10. Andrews, A.L. et al. (2002) J. Biol. Chem. 277:46073.
11. Tabata, Y. et al. (2007) Curr. Allergy Asthma Rep. 7:338.
12. Chiaramonte, M.G. et al. (2003) J. Exp. Med. 197:687.
13. Daines, M.O. and G.K. Hershey (2002) J. Biol. Chem. 227:10387.
14. Matsumura, M. et al. (2007) Biochem. Biophys. Res. Commun. 360:464.
15. Tabata, Y. et al. (2007) J. Immunol. 177:7905.
16. Andrews, A.L. et al. (2006) J. Allergy Clin. Immunol. 118:858.
17. Joshi, B.H. et al. (2006) Vitam. Horm. 74:479.
18. Andrews, A.-L. et al. (2007) J. Allergy Clin. Immunol. 120:91.

Bioinformatics

• Uniprot:
  • AAP93198()