LIF Human
Leukemia Inhibitory Factor Human Recombinant
Cat. No.
BT19022
Source
Escherichia Coli.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
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.
Shipped with Ice Packs 
In Stock 
Description
Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa.
The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Leukemia Inhibitory Factor (LIF) is a protein that plays a crucial role in maintaining embryonic stem cells and preventing them from differentiating. It also has various other functions, including influencing the development of certain nerve cells, regulating stem cell versatility, impacting bone and fat metabolism, stimulating the growth of specific cell types, and promoting the production of megakaryocytes (cells that produce platelets). The human and mouse versions of LIF share a 78% similarity in their amino acid sequence.
Description
Recombinant Human Leukemia Inhibitory Factor (LIF) is produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain consisting of 180 amino acids with a molecular weight of 19.7kDa. This LIF protein is purified using specialized chromatographic methods, resulting in a highly pure product.
Physical Appearance
White powder, sterilized by filtration and freeze-dried.
Formulation
The Leukemia Inhibitory Factor (LIF) is provided as a freeze-dried powder. It was initially dissolved in a sterile solution of phosphate-buffered saline (PBS) at a concentration of 1mg/ml and adjusted to a pH of 7.4 before freeze-drying.
Solubility
To reconstitute the freeze-dried Leukemia Inhibitory Factor (LIF), it is recommended to dissolve it in sterile water at a concentration of at least 100µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
The freeze-dried Leukemia Inhibitory Factor (LIF) remains stable at room temperature for up to 3 weeks. However, it is recommended to store it in a dry environment below -18°C for long-term storage. Once reconstituted, LIF should be stored at 4°C for up to 7 days. For extended storage, it's advisable to freeze it below -18°C. Adding a carrier protein such as HSA or BSA at 0.1% concentration can further enhance its stability during storage. Avoid repeated freezing and thawing cycles.
Purity
The purity of Leukemia Inhibitory Factor (LIF) is greater than 98% as determined by two different analytical methods: High-Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Biological Activity
The biological activity of Leukemia Inhibitory Factor (LIF) was assessed using the M1 cell differentiation assay. The ED50, which represents the concentration of LIF required to achieve 50% of the maximum biological response, was found to be less than 0.01 ng/ml. This translates to a specific activity of 100,000,000 International Units (IU) per milligram of protein.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Source
Escherichia Coli.
Amino Acid Sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
Product Science Overview
Discovery and History
LIF was discovered in the late 1980s by researchers at the Walter and Eliza Hall Institute in Melbourne, Australia. They isolated a protein from mouse Krebs tumor cells that could induce the differentiation of mouse myeloid leukemia cells into macrophages and granulocytes without promoting their proliferation . This protein was named Leukemia Inhibitory Factor due to its inhibitory effects on leukemia cell proliferation .
Structure and Expression
LIF is a glycoprotein with a molecular weight of approximately 20 kDa . It is expressed in various tissues and cell types, including the trophectoderm of the developing embryo, where it plays a crucial role in implantation and early embryonic development . The LIF receptor (LIFR) is a heterodimer composed of LIFR (gp190) and gp130, a common signal transducer for IL-6-type cytokines .
Biological Functions
LIF has a wide range of biological functions, including:
- Inducing differentiation: LIF can induce the terminal differentiation of various cell types, including myeloid leukemia cells and embryonic stem cells .
- Maintaining stem cell pluripotency: LIF is commonly used in the laboratory to maintain the undifferentiated state of mouse embryonic stem cells .
- Regulating immune responses: LIF can modulate immune responses by influencing the activity of various immune cells .
- Promoting cell survival: LIF has been shown to promote the survival of neurons and other cell types under stress conditions .
Recombinant Human LIF
Recombinant human LIF (hLIF) is produced using recombinant DNA technology, typically in bacterial or mammalian cell expression systems . It is used extensively in research and biotechnology for its ability to maintain the pluripotency of embryonic stem cells and its various other biological activities .
Applications in Research and Medicine
- Stem cell research: hLIF is widely used to maintain the undifferentiated state of mouse embryonic stem cells in culture .
- Cancer research: Due to its role in cell differentiation and survival, hLIF is studied for its potential therapeutic applications in cancer treatment .
- Neurobiology: hLIF is investigated for its neuroprotective effects and potential use in treating neurodegenerative diseases .
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