Human Fatty Acid-Binding Protein 1 (FABP1) is a cytoplasm protein, which belongs to the calycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP1 forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. FABP1 can bind free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm, so it can be involved in intracellular lipid transport.
LGALS7, also known as Galectin-7, is a member of the galectins family. The galectins are a family of beta-galactoside-binding proteins. There are at least 14 identified members of this family. Galectins share similarities in the CRD (the carbohydrate recognition domain). They are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or targeted to the nucleus. Galectins are implicated in modulating cell-cell and cell-matrix interactions. LGALS7 contains 1 galectin domain and is mainly expressed in stratified squamous epithelium. Galectin-7 could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. LGALS7 is a pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release.
Galectin-Related Protein (LGALSL) is a 172 amino acid protein that contains one Galectin domain. LGALSL does not appear to bind carbohydrates or lactose as the critical residues required for binding are not conserved. LGALSL may play a significant role in stimulating smooth muscle growth in developing alveolar wall vessels and the development of pulmonary capillaries.
Leukemia Inhibitory Factor (LIF) is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation; control of stem cell pluripotency; bone and fat metabolism; mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Human and murine mature LIF exhibit a 78% sequence identity at the amino acid level. Human LIF is equally active on human and mouse cells. Murine LIF is approximately 1000 fold less active on human cells than human LIF.
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