Recombinant Human Leukemia Inhibitory Factor Receptor (LIFR) Protein (hFc-Flag), Active

Beta LifeScience SKU/CAT #: BLC-05821P
Greater than 95% as determined by SDS-PAGE.
Greater than 95% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized human LIF at 2 μg/ml can bind human LIFR, the EC 50 is 11.68-15.52 ng/ml. Biological Activity Assay
Activity Measured by its binding ability in a functional ELISA. Immobilized human LIF at 2 μg/ml can bind human LIFR, the EC 50 is 11.68-15.52 ng/ml. Biological Activity Assay

Recombinant Human Leukemia Inhibitory Factor Receptor (LIFR) Protein (hFc-Flag), Active

Beta LifeScience SKU/CAT #: BLC-05821P
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Product Overview

Description Recombinant Human Leukemia Inhibitory Factor Receptor (LIFR) Protein (hFc-Flag), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity Greater than 95% as determined by SDS-PAGE.
Endotoxin Less than 1.0 EU/ug as determined by LAL method.
Activity Measured by its binding ability in a functional ELISA. Immobilized human LIF at 2 μg/ml can bind human LIFR, the EC 50 is 11.68-15.52 ng/ml.
Uniprotkb P42702
Target Symbol LIFR
Synonyms (LIF receptor)(LIF-R)(CD118)
Species Homo sapiens (Human)
Expression System Mammalian cell
Tag C-hFc-Flag
Target Protein Sequence QKKGAPHDLKCVTNNLQVWNCSWKAPSGTGRGTDYEVCIENRSRSCYQLEKTSIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNLSADFSTSTLYLKWNDRGSVFPHRSNVIWEIKVLRKESMELVKLVTHNTTLNGKDTLHHWSWASDMPLECAIHFVEIRCYIDNLHFSGLEEWSDWSPVKNISWIPDSQTKVFPQDKVILVGSDITFCCVSQEKVLSALIGHTNCPLIHLDGENVAIKIRNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETHDLKEIICSWNPGRVTALVGPRATSYTLVESFSGKYVRLKRAEAPTNESYQLLFQMLPNQEIYNFTLNAHNPLGRSQSTILVNITEKVYPHTPTSFKVKDINSTAVKLSWHLPGNFAKINFLCEIEIKKSNSVQEQRNVTIKGVENSSYLVALDKLNPYTLYTFRIRCSTETFWKWSKWSNKKQHLTTEASPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKAEIRLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGILLTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDEFRPGIRYNFFLYGCRNQGYQLLRSMIGYIEELAPIVAPNFTVEDTSADSILVKWEDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQKTLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENS
Expression Range 45-833aa
Protein Length Partial
Mol. Weight 119.3 kDa
Form Lyophilized powder
Buffer Lyophilized from a 0.2 μm filtered PBS, 6% Trehalose, pH 7.4
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.
Subcellular Location [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.
Protein Families Type I cytokine receptor family, Type 2 subfamily
Database References

HGNC: 6597

OMIM: 151443

KEGG: hsa:3977

STRING: 9606.ENSP00000263409

UniGene: PMID: 29751081

  • These data indicate that miR-377-3p suppressed adipogenesis of human bone marrow mesenchymal stem cells by targeting LIFR, which provides novel insights into the molecular mechanism of miRNA-mediated cellular differentiation. PMID: 29959592
  • High expression of LIFR is associated with preeclampsia. PMID: 29363569
  • LIFR attenuates tumor metastasis by suppressing YAP expression, suggesting that LIFR may serve as a potential target for clear cell renal cell carcinoma treatment. PMID: 29902078
  • Data show that lncRNA-CTD-2108O9.1 represses metastasis by targeting leukemia inhibitory factor receptor (LIFR). PMID: 29603493
  • Significant reduction in LIFR expression and the reduced activation of subsequent signaling strongly suggest a working model of how the implantation markers, LIF, may affect the endometrium of patients with adenomyosis. PMID: 27903796
  • Expression of cancer-specific glycan epitopes represents an excellent opportunity for diagnostics and potentially specific detection of tumors. Here, we report four proteins (LIFR, CE350, VP13A, HPT) found in sera from pancreatic cancer patients carrying aberrant glycan structures as compared to those of controls. PMID: 28244758
  • Authors demonstrate heterozygous novel or rare LIFR mutations in 3.3% of CAKUT patients, and provide evidence that Lifr deficiency and deactivating LIFR mutations cause highly similar anomalies of the urogenital tract in mice and humans. PMID: 28334964
  • LIFR inhibited the expression of beta-catenin. PMID: 27375070
  • The Leukemia Inhibitory Factor Receptor Gene Is a Direct Target of RUNX1 PMID: 26060100
  • We report the case of a girl with Stuve-Wiedemann syndrome confirmed on molecular analysis. PMID: 25868946
  • The C65S mutant LIFR showed altered glycosylation and an elevated expression level that might be attributed to a slow turnover of the mutant form. PMID: 26285796
  • High LIFr expression stimulates melanoma cell migration and is associated with unfavorable prognosis in melanoma. PMID: 26329521
  • Stuve-Wiedemann syndrome patients with (p.Arg692X) LIFR mutation may develop central adrenal insufficiency due to impaired LIF/LIFR signalling. LIF/LIFR system plays a role in human HPA axis regulation. PMID: 25145448
  • these findings conclude that LIFR functions as a novel metastasis suppressor in Hepatocellular carcinoma and may serve as a prognostic biomarker for Hepatocellular carcinoma patients. PMID: 26249360
  • LIFR may play a functional role in hepatocarcinogenesis PMID: 25749520
  • Expression of the LIF receptor was strongly increased on immune cells of multiple sclerosis patients. PMID: 25514345
  • The LIFRalpha-CT3 TAT fusion protein can inhibit miR-155 expression PMID: 25092123
  • LIFR signaling usually follows the JAK/STAT3 pathway, and is initiated by several interleukin-6-type cytokines PMID: 24618404
  • R28E mutation in CNTF abrogatesIL-6 receptor-dependent but retains CNTF receptor-dependent signaling via glycoprotein 130/ LIFR. PMID: 24802752
  • LIFR rs3729740 and possibly ANXA11 rs1049550 may be useful as biomarkers for predicting whether metastatic colorectal cancer patients are sensitive to relevant target regimens, although further validation in large cohorts is needed. PMID: 23579219
  • Because acute ventricle enlargement is observed in susceptible CD118-deficient mice, the phenomenon may occur in a subpopulation of human adults with herpes simplex encephalitis. PMID: 23382563
  • findings show that LIFR is a key novel tumor suppressor, whose deregulation may drive the transformation of a significant proportion of human breast cancers PMID: 22535017
  • findings identify LIFR as a metastasis suppressor that functions through the Hippo-YAP pathway and has significant prognostic power. PMID: 23001183
  • A unique loop structure in oncostatin M determines binding affinity toward oncostatin M receptor and leukemia inhibitory factor receptor. PMID: 22829597
  • A significant association was detected between the LIFR gene polymorphisms and schizophrenia patients with persecutory delusion PMID: 21971603
  • LIF and LIFR immunolocalized to decidual cells in the mid-late secretory phase endometrium and 1st trimester decidua. PMID: 21966484
  • These results demonstrate that cancer-specific methylation and a specific decrease of LIFR expression are a common inactivation event in colon cancer development. PMID: 21617854
  • Down regulation of Leukemia inhibitory factor receptor is associated with hepatocellular carcinoma. PMID: 19733004
  • The present study indicated that the LIF gene variant may produce susceptibility to hebephrenic schizophrenia and deterioration of working memory function. PMID: 19879916
  • Review. The structure and function of the LIF-R gene and protein, mRNA processing, and its role in tumor cells are reviewed. PMID: 11042511
  • upper cytokine-binding module and the Ig-like domain of the leukaemia inhibitory factor (LIF) receptor are sufficient for a functional LIF receptor complex PMID: 11812136
  • Separate functions for the two modules of the membrane-proximal cytokine binding domain of glycoprotein 190, the leukemia inhibitory factor low affinity receptor, in ligand binding and receptor activation (gp190) PMID: 11834739
  • interactions of CNTFR with LIFR and gp130 in vitro PMID: 12707266
  • mutations alter the stability of LIFR messenger RNA transcripts, resulting in the absence of the LIFR protein and in the impairment of the JAK/STAT3 signaling pathway in patient cells PMID: 14740318
  • immunocytochemical staining and mRNA expression of LIF and its receptor are consistent with the concept that LIF might be involved in growth initiation of human primordial follicles through its receptor PMID: 15044601
  • In cells overexpressing a LIFR mutant with the N-terminal cytokine binding domain deleted, signaling by ciliary neurotrophic factor was abolished. PMID: 16051226
  • Expression of leukemia inhibitory factor and its receptor is low in undifferentiated human embryonic stem cells but increases during differentiation. PMID: 16949591
  • sOSMR is able to bind OSM and interleukin-31 when associated to soluble gp130 or soluble interleukin-31R, respectively, and to neutralize both cytokine properties PMID: 17028186
  • Results present the biophysical and structural characterization of the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha). PMID: 18775332
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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