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

Name: Recombinant Human Leukemia Inhibitory Factor Receptor (LIFR) Protein (hFc-Flag), Active
Brand: Beta LifeScience
SKU: BLC-05821P
Availability: InStock

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

Collections: Cytokines, Recombinant proteins

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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: Hs.133421
Associated Diseases	Stueve-Wiedemann syndrome (STWS)

Gene Functions References

High levels of LIFR in colorectal cancer (CRC) facilitated proliferation and migration of endothelial cells, resulting in an increase in angiogenic activity. Moreover, IL-8 was found to play a role in the LIFR induced angiogenesis. IL-8 levels were correlated with LIFR levels in CRC tissues, whereas depletion of IL-8 led to a reduced angiogenic activity of LIFR in CRC cells. 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

FAQs

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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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.