Review



human lif (hlif)  (ORF Genetics)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    ORF Genetics human lif (hlif)
    Human Lif (Hlif), supplied by ORF Genetics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/human+lif++hlif+/pmc08634432-60-18-30
    Average 90 stars, based on 1 article reviews
    human lif (hlif) - by Bioz Stars, 2026-09
    90/100 stars

    Images

    Related Articles

    Recombinant:

    Article Title: CRISPR/Cas9 and Transgene Verification of Gene Involvement in Unfolded Protein Response and Recombinant Protein Production in Barley Grain
    Article Snippet: Commercial LIF recombinant protein is traditionally expressed in Escherichia coli ( E. coli ), but there is also recombinant human LIF (hLIF) on the market produced in rice (Merck), barley (ORF Genetics), and recombinant mouse LIF (mLIF) produced in barley (ORF Genetics).

    Produced:

    Article Title: CRISPR/Cas9 and Transgene Verification of Gene Involvement in Unfolded Protein Response and Recombinant Protein Production in Barley Grain
    Article Snippet: Commercial LIF recombinant protein is traditionally expressed in Escherichia coli ( E. coli ), but there is also recombinant human LIF (hLIF) on the market produced in rice (Merck), barley (ORF Genetics), and recombinant mouse LIF (mLIF) produced in barley (ORF Genetics).



    Similar Products

    hlif  (Cell Signaling Technology Inc)
    94
    Cell Signaling Technology Inc hlif
    Hlif, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/Human+LIF+Recombinant+Protein/pmc12805378-15-0-2
    Average 94 stars, based on 1 article reviews
    hlif - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier
    hlif  (R&D Systems)
    93
    R&D Systems hlif
    Hlif, 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
    https://www.bioz.com/product/human+lif+(hlif)/Recombinant+Human+LIF+Protein/pmc12683510-39-37-40
    Average 93 stars, based on 1 article reviews
    hlif - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier
    lif recombinant human protein (hlif  (Thermo Fisher)
    90
    Thermo Fisher lif recombinant human protein (hlif
    Lif Recombinant Human Protein (Hlif, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/pm35772103-23-44-49
    Average 90 stars, based on 1 article reviews
    lif recombinant human protein (hlif - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier
    hlif  (Proteintech)
    94
    Proteintech hlif
    Hlif, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/Animal-free+Recombinant+Human+LIF/pm35852463-369-23-28
    Average 94 stars, based on 1 article reviews
    hlif - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier
    human lif (hlif)  (PeproTech)
    90
    PeproTech human lif (hlif)
    Human Lif (Hlif), supplied by PeproTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/lif/pm34010985-140-11-14
    Average 90 stars, based on 1 article reviews
    human lif (hlif) - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier
    human lif (hlif)  (ORF Genetics)
    90
    ORF Genetics human lif (hlif)
    Human Lif (Hlif), supplied by ORF Genetics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/human+lif++hlif+/pmc08634432-60-18-30
    Average 90 stars, based on 1 article reviews
    human lif (hlif) - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier
    human leukemia inhibitor factor hlif  (Miltenyi Biotec)
    91
    Miltenyi Biotec human leukemia inhibitor factor hlif
    Human Leukemia Inhibitor Factor Hlif, 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
    https://www.bioz.com/product/human+lif+(hlif)/Human+LIF%2C+research+grade/pmc08393746-69-84-90
    Average 91 stars, based on 1 article reviews
    human leukemia inhibitor factor hlif - by Bioz Stars, 2026-09
    91/100 stars
    		  Buy from Supplier
    recombinant hlif his  (Sino Biological)
    93
    Sino Biological recombinant hlif his
    a Yeast-displayed eLIFR containing the CBM I–Ig-like–CBM II domains (blue circles) has a slightly higher affinity for LIF-His than eLIFR CBM I–Ig-like domains (gray squares). Data are the mean ± SD of triplicate measurements. Data from individual experiments are shown as faint symbols. b Schematic of hLIFR-Fc and eLIFR-Fc. The three N-terminal domains, CBM I–Ig-like–CBM II, are fused to an hIgG1 Fc-domain, with the engineered Ig-like domain shown in dark teal for eLIFR-Fc. c Versus hLIFR-Fc, eLIFR-Fc remains more strongly bound to yeast-displayed LIF after overnight incubation with soluble LIF competitor, indicating a slower off-rate. * P = 0.024, ** P = 0.0024 versus the corresponding hLIFR-Fc condition, two-tailed unpaired Student’s t test. Data are mean ± SD ( n = 3). d KinExA data showing <t>that</t> <t>recombinant</t> eLIFR-Fc (blue triangles) has higher affinity to soluble <t>hLIF-His</t> than hLIFR-Fc (brown circles). Data are the mean of duplicate measurements. Data from individual experiments are shown as faint symbols. e hLIFR-Fc, eLIFR-Fc (bivalent and one-arm), and D25 antibody compete LIF away from WT LIFR. ns not significant, P = 0.03 for one-arm eLIFR-Fc and P = 0.04 for eLIFR-Fc versus hLIFR-Fc, two-tailed unpaired Student’s t test. f Both hLIFR-Fc and eLIFR-Fc (bivalent and one-arm) compete LIF away from WT gp130, but the D25 mAb does not and appears to increase binding, perhaps due to complex stabilization or more avid LIF binding. P = 0.02, ** P = 0.006, or *** P < = 0.0002 versus hLIFR-Fc or eLIFR-Fc (as indicated), two-tailed unpaired Student’s t test. For e and f , data are mean ± SD ( n ≥ 3 independent experiments).
    Recombinant Hlif His, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/Human+LIF+Protein/pmc08041770-289-0-3
    Average 93 stars, based on 1 article reviews
    recombinant hlif his - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier
    hlif untagged  (Sino Biological)
    93
    Sino Biological hlif untagged
    a Yeast-displayed eLIFR containing the CBM I–Ig-like–CBM II domains (blue circles) has a slightly higher affinity for LIF-His than eLIFR CBM I–Ig-like domains (gray squares). Data are the mean ± SD of triplicate measurements. Data from individual experiments are shown as faint symbols. b Schematic of hLIFR-Fc and eLIFR-Fc. The three N-terminal domains, CBM I–Ig-like–CBM II, are fused to an hIgG1 Fc-domain, with the engineered Ig-like domain shown in dark teal for eLIFR-Fc. c Versus hLIFR-Fc, eLIFR-Fc remains more strongly bound to yeast-displayed LIF after overnight incubation with soluble LIF competitor, indicating a slower off-rate. * P = 0.024, ** P = 0.0024 versus the corresponding hLIFR-Fc condition, two-tailed unpaired Student’s t test. Data are mean ± SD ( n = 3). d KinExA data showing <t>that</t> <t>recombinant</t> eLIFR-Fc (blue triangles) has higher affinity to soluble <t>hLIF-His</t> than hLIFR-Fc (brown circles). Data are the mean of duplicate measurements. Data from individual experiments are shown as faint symbols. e hLIFR-Fc, eLIFR-Fc (bivalent and one-arm), and D25 antibody compete LIF away from WT LIFR. ns not significant, P = 0.03 for one-arm eLIFR-Fc and P = 0.04 for eLIFR-Fc versus hLIFR-Fc, two-tailed unpaired Student’s t test. f Both hLIFR-Fc and eLIFR-Fc (bivalent and one-arm) compete LIF away from WT gp130, but the D25 mAb does not and appears to increase binding, perhaps due to complex stabilization or more avid LIF binding. P = 0.02, ** P = 0.006, or *** P < = 0.0002 versus hLIFR-Fc or eLIFR-Fc (as indicated), two-tailed unpaired Student’s t test. For e and f , data are mean ± SD ( n ≥ 3 independent experiments).
    Hlif Untagged, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+lif+(hlif)/Human+LIF+Protein/pmc08041770-289-6-9
    Average 93 stars, based on 1 article reviews
    hlif untagged - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    a Yeast-displayed eLIFR containing the CBM I–Ig-like–CBM II domains (blue circles) has a slightly higher affinity for LIF-His than eLIFR CBM I–Ig-like domains (gray squares). Data are the mean ± SD of triplicate measurements. Data from individual experiments are shown as faint symbols. b Schematic of hLIFR-Fc and eLIFR-Fc. The three N-terminal domains, CBM I–Ig-like–CBM II, are fused to an hIgG1 Fc-domain, with the engineered Ig-like domain shown in dark teal for eLIFR-Fc. c Versus hLIFR-Fc, eLIFR-Fc remains more strongly bound to yeast-displayed LIF after overnight incubation with soluble LIF competitor, indicating a slower off-rate. * P = 0.024, ** P = 0.0024 versus the corresponding hLIFR-Fc condition, two-tailed unpaired Student’s t test. Data are mean ± SD ( n = 3). d KinExA data showing that recombinant eLIFR-Fc (blue triangles) has higher affinity to soluble hLIF-His than hLIFR-Fc (brown circles). Data are the mean of duplicate measurements. Data from individual experiments are shown as faint symbols. e hLIFR-Fc, eLIFR-Fc (bivalent and one-arm), and D25 antibody compete LIF away from WT LIFR. ns not significant, P = 0.03 for one-arm eLIFR-Fc and P = 0.04 for eLIFR-Fc versus hLIFR-Fc, two-tailed unpaired Student’s t test. f Both hLIFR-Fc and eLIFR-Fc (bivalent and one-arm) compete LIF away from WT gp130, but the D25 mAb does not and appears to increase binding, perhaps due to complex stabilization or more avid LIF binding. P = 0.02, ** P = 0.006, or *** P < = 0.0002 versus hLIFR-Fc or eLIFR-Fc (as indicated), two-tailed unpaired Student’s t test. For e and f , data are mean ± SD ( n ≥ 3 independent experiments).

    Journal: Communications Biology

    Article Title: An engineered ligand trap inhibits leukemia inhibitory factor as pancreatic cancer treatment strategy

    doi: 10.1038/s42003-021-01928-2

    Figure Lengend Snippet: a Yeast-displayed eLIFR containing the CBM I–Ig-like–CBM II domains (blue circles) has a slightly higher affinity for LIF-His than eLIFR CBM I–Ig-like domains (gray squares). Data are the mean ± SD of triplicate measurements. Data from individual experiments are shown as faint symbols. b Schematic of hLIFR-Fc and eLIFR-Fc. The three N-terminal domains, CBM I–Ig-like–CBM II, are fused to an hIgG1 Fc-domain, with the engineered Ig-like domain shown in dark teal for eLIFR-Fc. c Versus hLIFR-Fc, eLIFR-Fc remains more strongly bound to yeast-displayed LIF after overnight incubation with soluble LIF competitor, indicating a slower off-rate. * P = 0.024, ** P = 0.0024 versus the corresponding hLIFR-Fc condition, two-tailed unpaired Student’s t test. Data are mean ± SD ( n = 3). d KinExA data showing that recombinant eLIFR-Fc (blue triangles) has higher affinity to soluble hLIF-His than hLIFR-Fc (brown circles). Data are the mean of duplicate measurements. Data from individual experiments are shown as faint symbols. e hLIFR-Fc, eLIFR-Fc (bivalent and one-arm), and D25 antibody compete LIF away from WT LIFR. ns not significant, P = 0.03 for one-arm eLIFR-Fc and P = 0.04 for eLIFR-Fc versus hLIFR-Fc, two-tailed unpaired Student’s t test. f Both hLIFR-Fc and eLIFR-Fc (bivalent and one-arm) compete LIF away from WT gp130, but the D25 mAb does not and appears to increase binding, perhaps due to complex stabilization or more avid LIF binding. P = 0.02, ** P = 0.006, or *** P < = 0.0002 versus hLIFR-Fc or eLIFR-Fc (as indicated), two-tailed unpaired Student’s t test. For e and f , data are mean ± SD ( n ≥ 3 independent experiments).

    Article Snippet: Recombinant hLIF-His (14890-H08H-20, Sino Biological Inc.), hLIF (untagged) (14890-HNAH-50, Sino Biological Inc.), mLIF-His (ABIN2215872, Antibodies-Online), hOSM-His (10425-H08H-20, Sino Biological Inc.), and hCTF-1-Fc (16013-H01H-20, Sino Biological Inc.) were purchased for use.

    Techniques: Incubation, Two Tailed Test, Recombinant, Binding Assay

    a Yeast-displayed eLIFR containing the CBM I–Ig-like–CBM II domains (blue circles) has a slightly higher affinity for LIF-His than eLIFR CBM I–Ig-like domains (gray squares). Data are the mean ± SD of triplicate measurements. Data from individual experiments are shown as faint symbols. b Schematic of hLIFR-Fc and eLIFR-Fc. The three N-terminal domains, CBM I–Ig-like–CBM II, are fused to an hIgG1 Fc-domain, with the engineered Ig-like domain shown in dark teal for eLIFR-Fc. c Versus hLIFR-Fc, eLIFR-Fc remains more strongly bound to yeast-displayed LIF after overnight incubation with soluble LIF competitor, indicating a slower off-rate. * P = 0.024, ** P = 0.0024 versus the corresponding hLIFR-Fc condition, two-tailed unpaired Student’s t test. Data are mean ± SD ( n = 3). d KinExA data showing that recombinant eLIFR-Fc (blue triangles) has higher affinity to soluble hLIF-His than hLIFR-Fc (brown circles). Data are the mean of duplicate measurements. Data from individual experiments are shown as faint symbols. e hLIFR-Fc, eLIFR-Fc (bivalent and one-arm), and D25 antibody compete LIF away from WT LIFR. ns not significant, P = 0.03 for one-arm eLIFR-Fc and P = 0.04 for eLIFR-Fc versus hLIFR-Fc, two-tailed unpaired Student’s t test. f Both hLIFR-Fc and eLIFR-Fc (bivalent and one-arm) compete LIF away from WT gp130, but the D25 mAb does not and appears to increase binding, perhaps due to complex stabilization or more avid LIF binding. P = 0.02, ** P = 0.006, or *** P < = 0.0002 versus hLIFR-Fc or eLIFR-Fc (as indicated), two-tailed unpaired Student’s t test. For e and f , data are mean ± SD ( n ≥ 3 independent experiments).

    Journal: Communications Biology

    Article Title: An engineered ligand trap inhibits leukemia inhibitory factor as pancreatic cancer treatment strategy

    doi: 10.1038/s42003-021-01928-2

    Figure Lengend Snippet: a Yeast-displayed eLIFR containing the CBM I–Ig-like–CBM II domains (blue circles) has a slightly higher affinity for LIF-His than eLIFR CBM I–Ig-like domains (gray squares). Data are the mean ± SD of triplicate measurements. Data from individual experiments are shown as faint symbols. b Schematic of hLIFR-Fc and eLIFR-Fc. The three N-terminal domains, CBM I–Ig-like–CBM II, are fused to an hIgG1 Fc-domain, with the engineered Ig-like domain shown in dark teal for eLIFR-Fc. c Versus hLIFR-Fc, eLIFR-Fc remains more strongly bound to yeast-displayed LIF after overnight incubation with soluble LIF competitor, indicating a slower off-rate. * P = 0.024, ** P = 0.0024 versus the corresponding hLIFR-Fc condition, two-tailed unpaired Student’s t test. Data are mean ± SD ( n = 3). d KinExA data showing that recombinant eLIFR-Fc (blue triangles) has higher affinity to soluble hLIF-His than hLIFR-Fc (brown circles). Data are the mean of duplicate measurements. Data from individual experiments are shown as faint symbols. e hLIFR-Fc, eLIFR-Fc (bivalent and one-arm), and D25 antibody compete LIF away from WT LIFR. ns not significant, P = 0.03 for one-arm eLIFR-Fc and P = 0.04 for eLIFR-Fc versus hLIFR-Fc, two-tailed unpaired Student’s t test. f Both hLIFR-Fc and eLIFR-Fc (bivalent and one-arm) compete LIF away from WT gp130, but the D25 mAb does not and appears to increase binding, perhaps due to complex stabilization or more avid LIF binding. P = 0.02, ** P = 0.006, or *** P < = 0.0002 versus hLIFR-Fc or eLIFR-Fc (as indicated), two-tailed unpaired Student’s t test. For e and f , data are mean ± SD ( n ≥ 3 independent experiments).

    Article Snippet: Recombinant hLIF-His (14890-H08H-20, Sino Biological Inc.), hLIF (untagged) (14890-HNAH-50, Sino Biological Inc.), mLIF-His (ABIN2215872, Antibodies-Online), hOSM-His (10425-H08H-20, Sino Biological Inc.), and hCTF-1-Fc (16013-H01H-20, Sino Biological Inc.) were purchased for use.

    Techniques: Incubation, Two Tailed Test, Recombinant, Binding Assay