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Recombinant Human LIF, Animal-Free Protein

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Human LIF activity is determined using the LIF-responsive firefly luciferase reporter assay (*). HEK293T cells are treated in triplicate with a serial dilution of LIF overnight. Firefly luciferase activity is measured ...read more
Human LIF protein (Qk036) migrates as a single band at 20 kDa in non-reducing (NR) and upon reduction (R). Purified recombinant human LIF protein (3 μg) was resolved using 15% w/v SDS-PAGE in reduced (+ beta ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human LIF, Animal-Free Protein Summary

Details of Functionality
No significant difference between EC50 of reference and test lots
Source
E. coli-derived human LIF protein
Accession #
Protein/Peptide Type
Animal-Free Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
17 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
Monomeric human LIF protein only

Packaging, Storage & Formulations

Storage
Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
Buffer
Lyophilized from acetonitrile/TFA
Reconstitution Instructions
Resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

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

Alternate Names for Recombinant Human LIF, Animal-Free 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 widely expressed, highly and variably glycosylated, 32‑62 kDa, monomeric, pleiotropic cytokine in the IL‑6 family of helical cytokines (1‑4). The first exon encoding the signal sequence is alternately spliced, resulting in LIF-D, LIF-M, and LIF‑T mRNAs that produce secreted, extracellular matrix‑associated, and intracellular forms, respectively (5). LIF-D and LIF-M mRNAs produce identical 180 amino acid (aa) mature sequences (5). Mature human LIF (180 aa) shares 78%, 82%, 91%, 88 and 87% aa sequence identity with mouse, rat, canine, bovine, and porcine LIF, respectively. The LIF receptor is a heterodimer of a type I transmembrane ligand‑binding subunit, LIFR (gp190), and the type I transmembrane signal transducing subunit, gp130, signaling especially through STAT3 and JAK kinases (3, 4, 6). Gp130 and members of the LIFR family also mediate the biological effects of Oncostatin M, Cardiotrophin‑1, Galectin‑10, CNTF, IL‑6,
IL‑11, and IL‑27 (3, 6). A soluble LIFR has been reported in the mouse (7). Depending on the cells and their context, LIF either opposes or favors differentiation (3, 8). LIF produced by the uterine endometrium supports successful implantation of the embryo, promotes proliferation and maintenance of pluripotency in embryonic stem cells, and favors proliferation of progenitor cell types such as hematopoietic stem cells (3, 6, 8). However, excess LIF blocks differentiation of embryoid bodies, indicating the importance of LIF regulation (3, 6). LIF is produced by CD4+ T cells in response to activation, and is required by the thymic epithelium to support T cell maturation (3, 4). LIF expression is up‑regulated by neuronal injury, and promotes motor neuron survival and oligodendrocyte myelination (3, 4, 9). LIF is produced by the adrenal cortex and likely enhances its production of cortisol and aldosterone (10). LIF can function as an autocrine growth factor in some pancreatic cancers, but induces differentiation in the myeloid leukemic cell line M1 (2, 11). Tumor LIF can also induce formation of immunosuppressive tumor‑associated macrophages (12). LIF promotes endometrial remodeling and differentiation of adipocytes and cardiac smooth muscle cells (3, 4). It promotes regulatory T cell and inhibits Th17 cell differentiation, thus promoting tolerance, down‑regulating inflammation, and contributing to immune tolerance during pregnancy and in the nervous system (3, 4, 6, 8).

  1. Gough, N.M. et al. (1988) Proc. Natl. Acad. Sci. USA 85:2623.
  2. Moreau, J.F. et al. (1988) Nature 336:690.
  3. Trouillas, M. et al. (2009) Eur. Cytokine Netw. 20:51.
  4. Metcalfe, S.M. (2011) Genes Immun. 12:157.
  5. Voyle, R.B. et al. (1999) Exp. Cell Res. 249:199.
  6. Cheng, J.G. et al. (2001) Proc. Natl. Acad. Sci. USA 98:8680.
  7. Tomida, M. et al. (1993) FEBS lett. 334:193.
  8. Paiva, P. et al. (2009) Cytokine Growth Factor Rev. 20:319.
  9. Slaets, H. et al. (2010) Trends Mol. Med. 16:493.
  10. Bamberger, A.M. et al. (2000) Mol. Cell. Endocrinol. 162:145.
  11. Kamohara, H. et al. (2007) Int. J. Oncol. 30:977.
  12. Duluc, D. et al. (2007) Blood 110:4319.

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