Human LIF Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile 10 mM acetic acid at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
Once in solution, store at 4°C and use within 1 month, or store at -20ºC to -80ºC and use within 3 months to prevent loss of potency. Aliquot to avoid multiple freeze/thaw cycles if storing reconstituted material at -20ºC to -80ºC.
|Purity||A greater than or equal to 95% purity was determined by SDS-PAGE.|
|Endotoxin||Endotoxin levels are less than or equal to 1 EU / 1 μg hLIF.|
|Activity||The bioactivity of recombinant hLIF was determined in a TF-1 cell proliferation assay. The ED50 of each lot is less than or equal to 200 pg/ml.|
Recombinant human LIF was expressed in E. coli and is supplied in a lyophilized form.
Leukemia Inhibitory Factor (LIF) is a 20 kDa pleiotrophic factor belonging to the IL-6 superfamily of cytokines (1). LIF is expressed in a number of tissues and cell types. The LIF receptor is a heterodimer comprised of LIF-R (gp190) and gp130, a common signal transducer for IL-6-type cytokines (1). Depending on cell type and context, LIF/LIF-R can activate Erk, PI3K, and Jak1/Stat1/3 pathways (1,2). LIF has a diverse array of biological activities. Murine embryonic stem cells are dependent on LIF for pluripotency and self-renewal in vitro (1). Exercise-induced LIF secretion in muscle induces myoblast proliferation, suggesting that LIF may play a role in exercise-induced muscle hypertrophy (2). LIF also negatively regulates Th2 and Th17 cell differentiation (3,4).
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