Recombinant Human LIF, Biotinylated Protein Summary
Product Specifications
Pro24-Phe202
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
BT7734
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
BT7734/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Scientific Data
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Both Recombinant Biotinylated Human LIF (Catalog # BT7734) and unlabeled Recombinant Human LIF (Catalog # 7734-LF) induce TF-1 human erythroleukemic cell proliferation. The ED50 for this effect is 0.02-0.12 ng/mL. The similarity in activity highlights that the biotinylated protein is fully functional.
Reconstitution Calculator
Background: LIF
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).
- Gough, N.M. et al. (1988) Proc. Natl. Acad. Sci. USA 85:2623.
- Moreau, J.F. et al. (1988) Nature 336:690.
- Trouillas, M. et al. (2009) Eur. Cytokine Netw. 20:51.
- Metcalfe, S.M. (2011) Genes Immun. 12:157.
- Voyle, R.B. et al. (1999) Exp. Cell Res. 249:199.
- Cheng, J.G. et al. (2001) Proc. Natl. Acad. Sci. USA 98:8680.
- Tomida, M. et al. (1993) FEBS lett. 334:193.
- Paiva, P. et al. (2009) Cytokine Growth Factor Rev. 20:319.
- Slaets, H. et al. (2010) Trends Mol. Med. 16:493.
- Bamberger, A.M. et al. (2000) Mol. Cell. Endocrinol. 162:145.
- Kamohara, H. et al. (2007) Int. J. Oncol. 30:977.
- Duluc, D. et al. (2007) Blood 110:4319.
Citation for Recombinant Human LIF, Biotinylated Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Repositioning Mifepristone as a Leukaemia Inhibitory Factor Receptor Antagonist for the Treatment of Pancreatic Adenocarcinoma
Authors: C Di Giorgio, A Lupia, S Marchianò, M Bordoni, R Bellini, C Massa, G Urbani, R Roselli, F Moraca, V Sepe, B Catalanott, E Morretta, MC Monti, M Biagioli, E Distrutti, A Zampella, S Fiorucci
Cells, 2022-11-03;11(21):.
Species: Human
Sample Types: Protein
Applications: Bioassay
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