LIF Human, Sf9
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
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Product Science Overview
Leukemia Inhibitory Factor is a multifunctional cytokine that plays a crucial role in various biological processes. It is a member of the interleukin-6 cytokine family and is expressed in almost every tissue type within the body . The human recombinant form of Leukemia Inhibitory Factor, produced in Sf9 insect cells, has been widely used in research and therapeutic applications.
Leukemia Inhibitory Factor was first identified in the late 1960s when researchers observed that conditioned medium from normal cells could induce differentiation in murine myeloid leukemia cells . This factor was initially referred to as Differentiation Stimulating Factor or D-Factor. In 1987, Donald Metcalf and his team at the Walter and Eliza Hall Institute of Medical Research in Melbourne, Australia, isolated and characterized the protein, naming it Leukemia Inhibitory Factor due to its ability to inhibit the proliferation of leukemia cells .
Leukemia Inhibitory Factor is known for its diverse biological functions. It can enforce differentiation and suppress clonogenic self-renewal in various myeloid leukemic cell lines . In normal embryonic stem cells, it prevents differentiation commitment, maintaining their pluripotency . Additionally, Leukemia Inhibitory Factor has significant effects on a wide range of other cells, including hepatic parenchymal cells, neurons, adipocytes, osteoblasts, and gonadal cells .
Leukemia Inhibitory Factor exerts its effects by binding to a specific receptor complex on the cell surface, which includes the Leukemia Inhibitory Factor receptor and glycoprotein 130. This binding activates several intracellular signaling pathways, including the Janus kinase/signal transducer and activator of transcription pathway, the mitogen-activated protein kinase pathway, and the phosphatidylinositol 3-kinase pathway. These pathways mediate the diverse biological effects of Leukemia Inhibitory Factor, including cell differentiation, survival, and proliferation.
The human recombinant form of Leukemia Inhibitory Factor, produced in Sf9 insect cells, has been instrumental in various research and therapeutic applications. It is commonly used in the maintenance of pluripotency in embryonic stem cell cultures, allowing researchers to study stem cell biology and develop regenerative medicine therapies . Additionally, Leukemia Inhibitory Factor has potential therapeutic applications in treating conditions such as thrombocytopenia and myeloid leukemia .
