Recombinant Human IL-12 (Catalog # 10018-IL) stimulatesproliferation in PHA-activated human T lymphoblasts. The ED50 for this effectis 0.01-0.05 ng/mL.
2 μg/lane of Recombinant Human IL‑12 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 63-75 kDa.
Recombinant Human IL-12 (linked heterodimer) Protein, CF Summary
Additional Information
GS Linker, Defined heterodimer stoichiometry.
Details of Functionality
Measured in a cell proliferation assay using PHA-stimulated human T lymphoblasts. Symons, J.A. et al. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 272.
The ED50 for this effect is 0.01-0.05 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-12 protein
Human IL-12p40 (Ile23-Ser328) Accession # P29460.1
GSGSSRGGSGSGGSGGGGSK
Human IL-12p35 (Arg23-Ser219) Accession # P29459.2
>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
59 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
63-75 kDa, under reducing conditions.
Publications
Read Publications using 10018-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 (1). 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 (2, 3). These observations have led to the suggestion that IL-12
might have evolved from a cytokine/soluble receptor complex. Human and murine
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. IL-12 is
produced by macrophages and B lymphocytes and has been shown to have multiple
effects on T cells and natural killer (NK) cells (4). These effects include inducing
production of IFN-gamma and TNF by resting and activated T and NK cells,
synergizing with other IFN‑gamma inducers at both the transcriptional and
post-transcriptional levels. This interaction induces IFN-gamma gene
expression, enhancing the cytotoxic activity of resting NK and T cells,
inducing and synergizing with IL-2 in the generation of lymphokine-activated
killer (LAK) cells, acting as a co-mitogen to stimulate proliferation of
resting T cells, and inducing proliferation of activated T and NK cells (5).
Current evidence indicates that IL‑12, produced by macrophages in response to
infectious agents, is a central mediator of the cell‑mediated immune response by its actions on the
development, proliferation, and activities of TH1 cells. In its role as the
initiator of cell-mediated immunity, it has been suggested that IL-12 has
therapeutic potential as a stimulator of cell-mediated immune responses to
microbial pathogens, metastatic cancers, and viral infections such as AIDS.
Gubler, U. et al. (1991) Proc. Natl. Acad. Sci. 88:4143.
Gearing, D. et al. (1991) Cell 66:9.
Merberg, D. et al. (1992) Immunology Today 13:78.
Wolf, S.F. et al. (1991) Journal of Immunology 146:3074.
Airoldi, I. et al. (2000) Journal of Immunology 165:6880.
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