Human LIF (His Tag) recombinant protein
Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. It’s involved in growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation. LIF has potent proinflammatory property, being the inducer of the acute phase protein synthesis and affecting the cell recruitment into the area of damage or inflammation. LIF is also one of the cytokines that are capable to regulate the differentiation of embryonic stem cells, hematopoietic and neuronal cells. LIF binds to the specific LIF receptor (LIFR-α) which forms a heterodimer with a specific subunit common to all members of that family of receptors, the GP130 signal transducing subunit. This leads to activation of the JAK/STAT and MAPK cascades. Due to its polyfunctional activities, LIF is involved in the pathogenic events and development of many diseases of various origin.
Leukemia inhibitory factor
Protein short names
HILDA; MLPLI; RP23-329P17.1; DIA; D FACTOR; OTTMUSP00000005253; CDF
A DNA sequence encoding the human LIF (P15018) (Met1-Phe202) with a C-terminal polyhistidine tag was expressed.
The recombinant human LIF comprises 191 amino acids and has a predicted molecular mass of 21.2 kDa. The apparent molecular mass of the protein is approximately 35-42 kDa in SDS-PAGE under reducing conditions.
> 95 % as determined by SDS-PAGE
Measured by its ability to inhibit the proliferation of M1 mouse myeloid leukemia cells.
The ED50 for this effect is typically 0.2-1 ng/ml.
Human LIF Protein (His Tag) SDS-PAGE
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