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Recombinant Human IL-12/IL-23 p40 Protein, CF

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Recombinant Human IL-12/IL-23 p40 Protein (Catalog # 11407-IL) enhances IFN-gamma secretion in NK-92 human natural killer lymphoma cells. The ED50 for this effect is 2.00-20.0 ng/mL.
2 μg/lane of Recombinant Human IL‑12/IL‑23 p40 Protein (Catalog # 11407-IL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-12/IL-23 p40 Protein, CF Summary

Additional Information
(HEK293-Expressed)
Details of Functionality
Measured by its ability to enhance IFN-gamma secretion in NK-92 human natural killer lymphoma cells. The ED50 for this effect is 2.00-20.0 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-12/IL-23 p40 protein
Ile23-Ser328
Accession #
N-terminal Sequence
Ile23
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
35 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
38-45 kDa, under 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 Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute 10 μg size at 100 μg/mL and other sizes at 500 μg/mLin PBS.

Notes

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

Alternate Names for Recombinant Human IL-12/IL-23 p40 Protein, CF

  • CLMF p40
  • CLMF
  • CLMF2
  • Cytotoxic lymphocyte maturation factor 40 kDa subunit
  • IL12 p40
  • IL-12 p40
  • IL-12 subunit p40
  • IL12B
  • IL-12B
  • IL-12BNK cell stimulatory factor chain 2
  • interleukin 12, p40
  • interleukin 12B (natural killer cell stimulatory factor 2, cytotoxic lymphocytematuration factor 2, p40)
  • interleukin-12 beta chain
  • interleukin-12 subunit beta
  • natural killer cell stimulatory factor, 40 kD subunit
  • NKSF
  • NKSF2
  • NKSF2IL12, subunit p40

Background

Interleukin 12 (IL-12) is the founding member of the IL-12 family of heterodimeric cytokines, which have important immunological functions (1). It is a disulfide-linked, 70 kDa (p70) heterodimeric glycoprotein composed of a 40 kDa (p40) subunit and a 35 kDa (p35) subunit. Human IL-12p40 is a 40 kDa glycoprotein that shows considerable structural similarity to the extracellular domain of hematopoietin receptors (2). It is synthesized as a 328 amino acid (aa) precursor with a 22 aa signal sequence and a 306 aa mature region that contains a 92 aa fibronectin type III domain and an 84 aa Ig C2-like region and has a high degree of structural homology to type I cytokine receptors. There are two intrachain disulfide bonds and four potential N-linked glycosylation sites (3). Once made, it can exist in multiple forms including monomer, homodimer, heterodimer linked to p19 (forming IL-23), and heterodimer linked to p35 (forming IL-12) (1, 4, 5). Mature human IL-12p40 shows 66% aa sequence identity to mouse and rat IL-12p40 respectively. The secreted form of the p40 subunit inhibits IL-23 functions and abrogates IL-23-mediated anti-tumor effects (6). Characterization of the IL-12p40 proteins for binding and bioactivity showed that both the p40 monomer and dimer inhibited IL-12 binding to IL-12R (7).
  1. Trinchieri, G. et al. (2003) Immunity 19:641.
  2. Egwuagu, C. E. et al. (2015) Cytokine Growth Factor Rev. 26:587.
  3. Tone, Y. et al. (1996) Eur. J. Immunol. 26:1222.
  4. Lankford, C.S. and D.M. Frucht (2003) J. Leukoc. Biol. 73:49.
  5. Oppmann,B. et al. (2000) Immunity 13:715.
  6. Shimozato, O et al. (2005) Immunology 117:22.
  7. Ling, P et al. (1995) J. Immunol. 154:116.

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