human lif Search Results


91
Miltenyi Biotec human lif
Human Lif, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems recombinant human lif
Fig. 1 Design of the cytokimera GIL-11. a schematic illustration of the tetrameric and hexameric IL-11:IL-11R:gp130 receptor complex possibilities. IL-11 initially binds to IL-11R via site I. gp130 is recruited into this complex via major interactions between site III of IL-11 and D1 (Ig-like) of gp130 and site II of IL- 11 and D2/D3 (cytokine binding module (CBM)) of gp130. b schematic illustration of the trimeric <t>LIF:gp130:LIFR</t> complex. LIF binds via site III to D3/D4 of LIFR and via site II to D2/D3 of gp130. c schematic illustration of the tetrameric GIL-11:IL-11R:gp130:LIFR complex. GIL-11 binds via site III to D3/D4 of LIFR, via site II to D2/D3 of gp130 and via site I to D2/D3 of IL-11R. d schematic illustration (left) and space fill model (right) of the tetrameric GIL-11:IL- 11R:LIFR:gp130 (PDB 6O4P;11 2Q7N;83 1P9M10). GIL-11 binds via site I to IL-11R, via site II to gp130 and via site III to LIFR. e Combined transparent space fill/ band model of GIL-11, red: IL-11, green: exchanged region by LIF. f Structure-based schematic sequence alignment of hIL-11 (PDB 6O4O11), <t>hLIF</t> (PDB 1PVH33) and the resulting GIL-11. Site IIIa,b,c residues are highlighted in green and red boxes.
Recombinant Human Lif, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
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R&D Systems anti humanlif antibody
Fig. 1 Design of the cytokimera GIL-11. a schematic illustration of the tetrameric and hexameric IL-11:IL-11R:gp130 receptor complex possibilities. IL-11 initially binds to IL-11R via site I. gp130 is recruited into this complex via major interactions between site III of IL-11 and D1 (Ig-like) of gp130 and site II of IL- 11 and D2/D3 (cytokine binding module (CBM)) of gp130. b schematic illustration of the trimeric <t>LIF:gp130:LIFR</t> complex. LIF binds via site III to D3/D4 of LIFR and via site II to D2/D3 of gp130. c schematic illustration of the tetrameric GIL-11:IL-11R:gp130:LIFR complex. GIL-11 binds via site III to D3/D4 of LIFR, via site II to D2/D3 of gp130 and via site I to D2/D3 of IL-11R. d schematic illustration (left) and space fill model (right) of the tetrameric GIL-11:IL- 11R:LIFR:gp130 (PDB 6O4P;11 2Q7N;83 1P9M10). GIL-11 binds via site I to IL-11R, via site II to gp130 and via site III to LIFR. e Combined transparent space fill/ band model of GIL-11, red: IL-11, green: exchanged region by LIF. f Structure-based schematic sequence alignment of hIL-11 (PDB 6O4O11), <t>hLIF</t> (PDB 1PVH33) and the resulting GIL-11. Site IIIa,b,c residues are highlighted in green and red boxes.
Anti Humanlif Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems human recombinant protein lif 7734 lf
Fig. 1 Design of the cytokimera GIL-11. a schematic illustration of the tetrameric and hexameric IL-11:IL-11R:gp130 receptor complex possibilities. IL-11 initially binds to IL-11R via site I. gp130 is recruited into this complex via major interactions between site III of IL-11 and D1 (Ig-like) of gp130 and site II of IL- 11 and D2/D3 (cytokine binding module (CBM)) of gp130. b schematic illustration of the trimeric <t>LIF:gp130:LIFR</t> complex. LIF binds via site III to D3/D4 of LIFR and via site II to D2/D3 of gp130. c schematic illustration of the tetrameric GIL-11:IL-11R:gp130:LIFR complex. GIL-11 binds via site III to D3/D4 of LIFR, via site II to D2/D3 of gp130 and via site I to D2/D3 of IL-11R. d schematic illustration (left) and space fill model (right) of the tetrameric GIL-11:IL- 11R:LIFR:gp130 (PDB 6O4P;11 2Q7N;83 1P9M10). GIL-11 binds via site I to IL-11R, via site II to gp130 and via site III to LIFR. e Combined transparent space fill/ band model of GIL-11, red: IL-11, green: exchanged region by LIF. f Structure-based schematic sequence alignment of hIL-11 (PDB 6O4O11), <t>hLIF</t> (PDB 1PVH33) and the resulting GIL-11. Site IIIa,b,c residues are highlighted in green and red boxes.
Human Recombinant Protein Lif 7734 Lf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Novus Biologicals recombinant human lif protein
Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of <t>LIF</t> at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of <t>recombinant</t> human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.
Recombinant Human Lif Protein, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems anti lif
Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of <t>LIF</t> at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of <t>recombinant</t> human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.
Anti Lif, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems leukaemia inhibitory factor lif
Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of <t>LIF</t> at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of <t>recombinant</t> human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.
Leukaemia Inhibitory Factor Lif, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems leukemia inhibitory factor lif
Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of <t>LIF</t> at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of <t>recombinant</t> human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.
Leukemia Inhibitory Factor Lif, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
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93
Proteintech human leukemia inhibitory factor
Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of <t>LIF</t> at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of <t>recombinant</t> human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.
Human Leukemia Inhibitory Factor, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems lif biotinylated
Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of <t>LIF</t> at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of <t>recombinant</t> human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.
Lif Biotinylated, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems lif staining
A–D. <t>LIF</t> immunolocalized strongly to the decidua (d) and also to the luminal epithelium (le). E–H. LIFR immunolocalized strongly to the decidua. Bottom row, negative controls to sections above. The same negative is shown for <t>both</t> <t>antibodies</t> as the primary antibodies shown were both raised in goat. n = 3; m. myometrium; s, stroma.
Lif Staining, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Fig. 1 Design of the cytokimera GIL-11. a schematic illustration of the tetrameric and hexameric IL-11:IL-11R:gp130 receptor complex possibilities. IL-11 initially binds to IL-11R via site I. gp130 is recruited into this complex via major interactions between site III of IL-11 and D1 (Ig-like) of gp130 and site II of IL- 11 and D2/D3 (cytokine binding module (CBM)) of gp130. b schematic illustration of the trimeric LIF:gp130:LIFR complex. LIF binds via site III to D3/D4 of LIFR and via site II to D2/D3 of gp130. c schematic illustration of the tetrameric GIL-11:IL-11R:gp130:LIFR complex. GIL-11 binds via site III to D3/D4 of LIFR, via site II to D2/D3 of gp130 and via site I to D2/D3 of IL-11R. d schematic illustration (left) and space fill model (right) of the tetrameric GIL-11:IL- 11R:LIFR:gp130 (PDB 6O4P;11 2Q7N;83 1P9M10). GIL-11 binds via site I to IL-11R, via site II to gp130 and via site III to LIFR. e Combined transparent space fill/ band model of GIL-11, red: IL-11, green: exchanged region by LIF. f Structure-based schematic sequence alignment of hIL-11 (PDB 6O4O11), hLIF (PDB 1PVH33) and the resulting GIL-11. Site IIIa,b,c residues are highlighted in green and red boxes.

Journal: Communications biology

Article Title: Cytokimera GIL-11 rescued IL-6R deficient mice from partial hepatectomy-induced death by signaling via non-natural gp130:LIFR:IL-11R complexes.

doi: 10.1038/s42003-023-04768-4

Figure Lengend Snippet: Fig. 1 Design of the cytokimera GIL-11. a schematic illustration of the tetrameric and hexameric IL-11:IL-11R:gp130 receptor complex possibilities. IL-11 initially binds to IL-11R via site I. gp130 is recruited into this complex via major interactions between site III of IL-11 and D1 (Ig-like) of gp130 and site II of IL- 11 and D2/D3 (cytokine binding module (CBM)) of gp130. b schematic illustration of the trimeric LIF:gp130:LIFR complex. LIF binds via site III to D3/D4 of LIFR and via site II to D2/D3 of gp130. c schematic illustration of the tetrameric GIL-11:IL-11R:gp130:LIFR complex. GIL-11 binds via site III to D3/D4 of LIFR, via site II to D2/D3 of gp130 and via site I to D2/D3 of IL-11R. d schematic illustration (left) and space fill model (right) of the tetrameric GIL-11:IL- 11R:LIFR:gp130 (PDB 6O4P;11 2Q7N;83 1P9M10). GIL-11 binds via site I to IL-11R, via site II to gp130 and via site III to LIFR. e Combined transparent space fill/ band model of GIL-11, red: IL-11, green: exchanged region by LIF. f Structure-based schematic sequence alignment of hIL-11 (PDB 6O4O11), hLIF (PDB 1PVH33) and the resulting GIL-11. Site IIIa,b,c residues are highlighted in green and red boxes.

Article Snippet: Recombinant human OSM (catalog no. 295-OM) and recombinant human LIF (catalog no. 7734-LF) were purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Binding Assay, Sequencing

Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of LIF at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of recombinant human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.

Journal: Molecular Medicine Reports

Article Title: Expression and effects of leukemia inhibitory factor on nucleus pulposus degeneration

doi: 10.3892/mmr.2019.9874

Figure Lengend Snippet: Protein expression of aggrecan and COL2α1 in human nucleus pulposus cells stimulated with various concentrations of LIF at different durations. (A and B) Aggrecan and COL2α1 protein expression in human nucleus pulposus cells treated with various concentrations of recombinant human LIF protein. (C and D) Protein expression levels of aggrecan and COL2α1 in human nucleus pulposus cells treated with 100 ng/ml recombinant human LIF protein for various durations. (E) Toluidine blue staining following treatment of human nucleus pulposus cells with 0 or 100 ng/ml recombinant human LIF protein for 48 h. Data are presented as the means ± standard deviation. *P<0.05. COL2α1, collagen type II α1; LIF, leukemia inhibitory factor.

Article Snippet: Recombinant Human LIF Protein was purchased from Novus Biologicals, LLC (Littleton, CO, USA).

Techniques: Expressing, Recombinant, Staining, Standard Deviation

Effects of LIF on the proliferation and apoptosis of nucleus pulposus cells. (A and B) Apoptotic rate of human nucleus pulposus cells treated with various concentrations of recombinant human LIF. (C) Proliferation of human nucleus pulposus cells treated with various concentrations of recombinant human LIF. Data are presented as the means ± standard deviation. *P<0.05. FITC, fluorescein isothiocyanate; LIF, leukemia inhibitory factor; OD, optical density.

Journal: Molecular Medicine Reports

Article Title: Expression and effects of leukemia inhibitory factor on nucleus pulposus degeneration

doi: 10.3892/mmr.2019.9874

Figure Lengend Snippet: Effects of LIF on the proliferation and apoptosis of nucleus pulposus cells. (A and B) Apoptotic rate of human nucleus pulposus cells treated with various concentrations of recombinant human LIF. (C) Proliferation of human nucleus pulposus cells treated with various concentrations of recombinant human LIF. Data are presented as the means ± standard deviation. *P<0.05. FITC, fluorescein isothiocyanate; LIF, leukemia inhibitory factor; OD, optical density.

Article Snippet: Recombinant Human LIF Protein was purchased from Novus Biologicals, LLC (Littleton, CO, USA).

Techniques: Recombinant, Standard Deviation

A–D. LIF immunolocalized strongly to the decidua (d) and also to the luminal epithelium (le). E–H. LIFR immunolocalized strongly to the decidua. Bottom row, negative controls to sections above. The same negative is shown for both antibodies as the primary antibodies shown were both raised in goat. n = 3; m. myometrium; s, stroma.

Journal: PLoS ONE

Article Title: Leukemia Inhibitory Factor Enhances Endometrial Stromal Cell Decidualization in Humans and Mice

doi: 10.1371/journal.pone.0025288

Figure Lengend Snippet: A–D. LIF immunolocalized strongly to the decidua (d) and also to the luminal epithelium (le). E–H. LIFR immunolocalized strongly to the decidua. Bottom row, negative controls to sections above. The same negative is shown for both antibodies as the primary antibodies shown were both raised in goat. n = 3; m. myometrium; s, stroma.

Article Snippet: LIF and LIFR were immunolocalised as described above except that the non-immune block used was: LIF: 10% normal goat plus 2% normal mouse serum and LIFR: 10% normal horse and 2% mouse serum; and two LIF antibodies were used to confirm the specificity of LIF staining (rabbit anti-human LIF antibody as above and in and goat anti-human LIF antibody, R&D systems; 10 μg/ml).

Techniques: