Recombinant Feline IL-12/IL-23 p40 Protein

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Product Details

Summary
Reactivity FeSpecies Glossary
Applications Binding Activity

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Recombinant Feline IL-12/IL-23 p40 Protein Summary

Details of Functionality
Measured by its ability to compete with biotinylated feline IL-12/IL-23 p40 for binding with immobilized rhIL-12 R beta 1/Fc Chimera in a functional ELISA assay.
Source
Mouse myeloma cell line, NS0-derived feline IL-12/IL-23 p40 protein
Ile23-Ser329 (Glu167Gly), with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ile23
Protein/Peptide Type
Recombinant Proteins
Gene
IL12A
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
36 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
42 kDa and 45 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 °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.
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 sterile 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 Feline IL-12/IL-23 p40 Protein

  • CLMF2
  • IL12 p40
  • IL-12 p40
  • IL12B
  • IL-12B
  • NKSF2

Background

Interleukin 12 (IL-12) and IL-23 are secreted heterodimeric glycoproteins belonging to the IL-12 cytokine family. The two cytokines share a common p40 (40 kDa) subunit, which is disulfide-linked with the p35 (35 kDa) subunit in IL-12, and with the p19 (19 kDa) subunit in IL-23. Feline p40 is synthesized as a 329 amino acid (aa) precursor with a 22 aa signal sequence and a 307 aa mature region. It contains a 90 aa fibronectin type III domain and a 75 aa Ig C2-like region. The expression of p40 is induced by substances such as LPS and CpG that activate antigen-presenting cells. Besides being found as a component of IL-12 or IL-23, free p40 monomers and homodimers are also secreted by cells expressing p40. Feline p40 shares 94%, 85%, 84%, 65%, and 65% aa sequence identity with canine, human, porcine, rat and mouse p40, respectively. Cells known to express p40 include macrophages, dendritic cells, monocytes, Langerhans cells, neutrophils, keratinocytes, plasmacytoid dendritic cells, and microglia. From cells that express both the p35 and p40 subunits (dendritic cells, monocytes, and CHO cells), the amount of free p40 secreted is 10 - 1000 fold more than the heterodimeric IL-12. The high-affinity IL-12 receptor complex that transduces IL-12 signals is composed of a 100 kDa ligand-binding subunit (IL-12 R beta 1) and a 130-kDa signal transducing subunit (IL-12 R beta 2). Similarly, the high-affinity IL-23 signaling receptor complex is composed of the shared IL-12 R beta 1 and the unique IL-23 R, a novel gp130-like protein. Both the monomeric and the dimeric free p40 can bind to the IL-12 R beta 1 and function as antagonists of IL-12 or IL-23. However, the monomeric p40 binds IL-12 R beta 1 with lower affinity and is less potent as an IL-12 antagonist. Homodimeric mouse p40 has also been shown to have agonistic functions similar to IL-12, inducing nitric oxide expression and NF kappa B activation in mouse primary microglia and peritoneal macrophages. The molecular mechanism for the agonistic effects of homodimeric p40 has not been determined (1 - 6).

  1. Buttner, M. et al. (1997) Cytokine 10:241.
  2. Park, A.Y. and P. Scott (2001) Scand. J. Immunol. 53:529. 
  3. Trinchieri, G. et al. (2003) Immunity 19:641. 
  4. Brombacher, F. et al. (2003) Trends Immunol. 24:207.
  5. Lankford, C.S. and D.M. Frucht, 2003, J. Leukoc. Biol. 73:49.
  6. Abdi, K. (2002) Scand. J. Immunol. 5:1.

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Bioinformatics

Gene Symbol IL12A
Entrez
Uniprot