When Recombinant Human IL-12 R beta 1 Fc Chimera (Catalog # 839-B1) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human IL-12/IL-23 p40 Subunit (Catalog # 309-IL) binds with an ED50 of 1-6 ng/mL.
Recombinant Human IL-12/IL-23 p40 Subunit Protein Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When
Recombinant
Human IL‑12 R beta 1 Fc Chimera (Catalog # 839-B1)
is immobilized at 1 µg/mL (100
µL/well), the concentration of
Recombinant Human IL‑12/IL‑23 p40 Subunit that produces 50% of the
optimal binding response is 1-6 ng/mL.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human IL-12/IL-23 p40 protein Ile23-Ser328
>90%, 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
Dilutions
Bioactivity
Theoretical MW
34.7 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
40 kDa, reducing conditions
Publications
Read Publications using 309-IL in the following applications:
Interleukin 12, also known as natural killer cell stimulatory factor (NKSF) or cytotoxic lymphocyte maturation factor (CLMF), is a pleiotropic cytokine originally identified in the medium of activated human B lymphoblastoid cell lines. IL-12 is produced by macrophages and B lymphocytes and has multiple effects on T cells and NK cells, including stimulation of cytotoxic activity, proliferation, and promotion of Th1 development as well as IFN-gamma and TNF production. IL-12 is a disulfide-linked, 70 kDa (p70) heterodimeric glycoprotein composed of a 40 kDa (p40) subunit and a 35 kDa (p35) subunit. The p40 and p35 subunits by themselves have no IL-12 activity, the p40 dimer has been shown to bind the IL-12 receptor and to be an IL-12 antagonist. Free p35 has not been detected in supernatant solutions of cultured cells expressing only p35 or both p35 and p40 mRNAs. In contrast, p40 is secreted in excess of IL-12 in cells expressing both p35 and p40 mRNAs. The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the human IL-6 receptor while the p35 subunit shows distant but significant sequence similarity to IL-6, G-CSF, and chicken MGF. These observations have led to the suggestion that IL-12 might have evolved from a cytokine/soluble receptor complex. Human and mouse IL-12 share 70% and 60% amino acid sequence homology in their p40 and p35 subunits, respectively. IL-12 apparently shows species specificity with human IL-12 reportedly showing minimal activity in the murine system.
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