LIFR Mouse
Sf9, Baculovirus cells.
Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.
Greater than 90.0% as determined by SDS-PAGE.
Description
LIFR Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 794 amino acids (44-828 aa) and having a molecular mass of 89.6kDa.
LIFR is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
The Leukemia Inhibitory Factor Receptor Alpha (LIFR) protein belongs to the Interleukin-6 receptor family. LIFR mediates the actions of various proteins, including IL-6, IL-11, IL-27, and Oncostatin M, influencing cell proliferation, differentiation, and survival throughout different life stages. LIFR expression is often downregulated in various breast cancer types, making it a potential prognostic marker.
Recombinant Mouse LIFR, produced in Baculovirus, is a single, glycosylated polypeptide chain. It consists of 794 amino acids (44-828 aa), resulting in a molecular weight of 89.6kDa. The LIFR protein is engineered with a 9 amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.
The LIFR protein solution has a concentration of 0.25mg/ml and is prepared in a solution containing 10% glycerol and Phosphate-Buffered Saline with a pH of 7.4.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. It's important to minimize repeated freeze-thaw cycles to maintain product integrity.
The purity of the LIFR protein is determined by SDS-PAGE analysis and is greater than 90.0%.
The biological activity of LIFR is assessed based on its ability to inhibit the proliferation of TF-1 human erythroleukemic cells. The ED50 range, in the presence of Mouse LIF, is approximately less than or equal to 1ug/ml.
Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.
Sf9, Baculovirus cells.
ADPLKRGVQD LKCTTNNMRV WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSHH HHHH.
Product Science Overview
Leukemia Inhibitory Factor Receptor Alpha (LIFRα) is a critical component of the cytokine receptor family, specifically the interleukin-6 (IL-6) receptor family. This receptor plays a significant role in various biological processes, including cell growth, differentiation, and survival. The recombinant form of LIFRα, particularly from mouse models, has been extensively studied to understand its functions and applications in biomedical research.
LIFRα is a type I transmembrane protein with a molecular weight of approximately 190 kDa . It is also known as CD118 and is characterized by its ability to bind to the Leukemia Inhibitory Factor (LIF), a cytokine that influences cell growth by inhibiting differentiation . The receptor forms a heterodimer with the glycoprotein 130 (gp130) subunit, which is common to all IL-6 family members . This heterodimerization is crucial for the activation of various intracellular signaling pathways, including the Janus kinase/signal transducer and activator of transcription (JAK/STAT) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the phosphoinositide 3-kinase (PI3K) pathway .
LIFRα is involved in numerous physiological processes. It is essential for embryonic development, neural differentiation, bone metabolism, and inflammation . In the context of stem cell research, LIFRα is particularly important for maintaining the pluripotency of embryonic stem cells. The receptor’s interaction with LIF prevents the differentiation of these cells, thereby promoting their self-renewal . This property is exploited in stem cell culture systems, where recombinant LIF is added to the culture media to maintain the undifferentiated state of stem cells .
The recombinant form of mouse LIFRα has been produced to facilitate various research applications. Recombinant proteins are typically generated using expression systems such as bacteria, yeast, or mammalian cells. These systems allow for the production of large quantities of the protein, which can then be purified and used in experimental studies . Recombinant LIFRα is used to study the receptor’s structure-function relationships, signaling mechanisms, and interactions with other proteins. Additionally, it serves as a valuable tool in drug discovery and development, particularly in identifying potential therapeutic targets for diseases involving aberrant LIFRα signaling .
Understanding the role of LIFRα in disease has significant clinical implications. Dysregulation of LIFRα signaling has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders . For instance, aberrant activation of the LIFRα/STAT3 pathway has been associated with tumor progression and resistance to apoptosis in certain cancers . Consequently, targeting LIFRα or its downstream signaling components presents a potential therapeutic strategy for these diseases.
