Mouse LIF Antibody

Leukemia inhibitory factor (LIF) was initially identified as a factor that inhibited the proliferation and induced the differentiation to macrophages of the murine myeloid leukemic cell line M1. Subsequent to its purification and molecular cloning, LIF was recognized to be a pleiotropic factor with multiple effects on both hematopoietic and non-hematopoietic cells. LIF has overlapping biological functions with OSM, IL-6, IL-11 and CNTF. All these cytokines utilize gp130 as a component in their signal transducing receptor complexes. Mouse LIF cDNA encodes a 203 amino acid residue polypeptide with a 23 amino acid signal peptide that is cleaved to yield a 180 amino acid mature mouse LIF. Native human and mouse LIF are highly glycosylated monomeric proteins. Both human and murine LIF protein sequences have multiple potential N- and O-linked glycosylation sites and six conserved cysteine residues that are involved in three intramolecular disulfide bridges.