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Recombinant Canine LIF Protein

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Product Details

Summary
Reactivity CaSpecies Glossary
Applications Bioactivity

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Recombinant Canine LIF Protein Summary

Details of Functionality
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 0.02-0.12 ng/mL.
Source
E. coli-derived canine LIF protein
Pro24-Phe202
Accession #
N-terminal Sequence
Pro24
Protein/Peptide Type
Recombinant Proteins
Gene
LIF
Purity
>95%, by SDS-PAGE with silver staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
20 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
20 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 with silver staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Canine LIF Protein

  • CDF
  • D Factor
  • DIA
  • differentiation inhibitory activity
  • differentiation stimulating factor
  • Differentiation-stimulating factor
  • Emfilermin
  • HILDA
  • HILDAcholinergic differentiation factor
  • leukemia inhibitory factor (cholinergic differentiation factor)
  • leukemia inhibitory factor
  • LIF
  • Melanoma-derived LPL inhibitor
  • MLPLI

Background

LIF (leukemia inhibitory factor) is a 32-62 kDa, variably glycosylated, monomeric member of the IL-6 family of helical cytokines (1-4). LIF is widely expressed and highly pleiotropic. It is important for many physiological processes including embryo implantation and development, hematopoiesis, bone metabolism, and inflammation (5). Canine LIF is synthesized as a 202 amino acid (aa) precursor protein with a 22 aa signal sequence that can be alternately spliced to produce a secreted (LIF-D), extracellular matrix-associated (LIF-M), or intracellular (LIF-T) isoform (6). LIF-D and LIF-M have identical 180 aa mature sequences (6). Mature canine LIF shares 91% sequence identity with human LIF, 80% sequence identity with mouse and rat LIF, and 91% identity with bovine and porcine LIF. LIF induces signaling through a cell surface heterodimeric receptor complex composed of a ligand binding subunit (LIF R) and a 130 kDa signal transducing subunit (gp130). The gp130 subunit does not bind LIF by itself, but is required for high-affinity binding of LIF by the complex. LIF has been shown to support embryo implantation and to promote immunosuppression during pregnancy (7, 8). During development, it regulates cell proliferation and differentiation. However, its ability to favor or oppose either of these events is cell and context dependent (4, 5). LIF is important in the proliferation and maintenance of canine embryonic stem cells and induced pluripotent stem cells (9-11). LIF is up-regulated in activated CD4+ T cells, promotes regulatory T cell differentiation, and inhibits Th17 cell function (2, 5, 12). In the brain, it is up-regulated by neuronal injury and promotes neuron survival and oligodendrocyte myelination (2, 4, 13). It is produced by the adrenal cortex and enhances adrenal production of cortisol and aldosterone (14). Tumor cell-derived LIF has been shown to promote the differentiation of monocytes into tumor-associated macrophages (15, 16). LIF also promotes endometrial remodeling and the differentiation of adipocytes and cardiac smooth muscle cells (2, 4, 5).
  1. Gough, N.M. et al. (1988) Proc. Natl. Acad. Sci. U S A 85:2623.
  2. Metcalfe, S.M. (2011) Genes Immun. 12:157.
  3. Moreau, J.F. et al. (1988) Nature 336:690.
  4. Trouillas, M. et al. (2009) Eur. Cytokine Netw. 20:51.
  5. Mathieu, M.E. et al. (2012) Stem Cell Rev. 8:1.
  6. Voyle, R.B. et al. (1999) Exp. Cell. Res. 249:199.
  7. Paiva, P. et al. (2009) Cytokine Growth Factor Rev. 20:319.
  8. Cheng, J.G. et al. (2001) Proc. Natl. Acad. Sci. U S A 98:8680.
  9. Koh, S. et al. (2013) Stem Cells Dev. 22:951.
  10. Whitworth, D.J. et al. (2012) Stem Cells Dev. 21:2288.
  11. Luo, J. et al. (2011) Stem Cells Dev. 20:1669.
  12. Cao, W. et al. (2011) Immunity 35:273.
  13. Slaets, H. et al. (2010) Trends Mol. Med. 16:493.
  14. Bamberger, A.M. et al. (2000) Mol. Cell. Endocrinol. 162:145.
  15. Duluc, D. et al. (2007) Blood 110:4319.
  16. Kamohara, H. et al. (2007) Int. J. Oncol. 30:977.

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Bioinformatics

Gene Symbol LIF
Uniprot