Analytical Data
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Gene name
LIFR
- Application
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Alternative Names
CD118; SJS2; STWS; SWS
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
O70535
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Expression Region
Glu382~Ser486
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Molecular Weight
11kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
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Protein Description
LIFR (Leukemia Inhibitory Factor Receptor) is a key component of the signaling pathway activated by leukemia inhibitory factor (LIF), a cytokine associated with various biological processes, including stem cell maintenance, differentiation, and inflammation. The role of LIFR in these processes has drawn significant interest in the fields of developmental biology and regenerative medicine. Moreover, LIFR has been implicated in several pathological conditions, including cancer and autoimmune diseases, making it a potential target for therapeutic interventions. Research has focused on the characterization of LIFR in both normal and diseased states, revealing its importance in cellular responses to LIF and its potential implications in cell signaling pathways that regulate cell fate. Furthermore, the recombinant expression of LIFR allows for detailed studies of its functional properties and interaction with other molecules. By producing LIFR in a controlled environment, researchers can explore the receptor’s structural characteristics, assess ligand-binding dynamics, and evaluate downstream signaling effects. Understanding LIFR's mechanism of action could lead to novel strategies for manipulating stem cell behavior and developing new treatments for diseases associated with dysregulated LIFR signaling. Thus, ongoing research into LIFR and its recombinant protein forms is crucial for advancing our knowledge of cell signaling and its applications in biotechnology and medicine.
