Recombinant Canine IL-5 Protein

Catalog #: 1964-CL Datasheet / COA / SDS

Carrier Free

Catalog #	Availability	Size / Price	Qty
1964-CL-025/CF

With Carrier

Catalog #	Availability	Size / Price	Qty
1964-CL-025

R&D Systems Recombinant Proteins and Enzymes

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Product Details

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Canine IL-5 Protein Summary

Product Specifications

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Activity

Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED₅₀ for this effect is 2.00-8.00 ng/mL.

Source

Mouse myeloma cell line, NS0-derived canine IL-5 protein
Phe20-Ser134, with a C-terminal 6-His tag

Accession #

Q95J76

N-terminal Sequence
Analysis

Phe20

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

14.1 kDa (monomer)

SDS-PAGE

19-21 kDa, reducing conditions

Product Datasheets

1964-CL (with carrier)

Product Datasheet

COA

SDS

1964-CL/CF (carrier free)

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

1964-CL

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution	Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

1964-CL/CF

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 100 μg/mL in sterile PBS.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Reconstitution Calculator

Background: IL-5

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). Canine IL‑5 is synthesized as a 134 amino acid (aa) precursor that contains a 21 aa signal sequence and a 113 aa mature segment. Mature canine IL‑5 shares 62%, 58%, 56%, 83%, 84% and 85%, aa sequence identity with human, mouse, rat, equine, 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).

References

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.
Denburg, J. A. et al. (1991) Blood 77:1462.

Long Name

Interleukin 5

Entrez Gene IDs

3567 (Human); 16191 (Mouse); 24497 (Rat); 397409 (Porcine); 280825 (Bovine); 403790 (Canine); 493803 (Feline)

Alternate Names

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