- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-644
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.
Solubility
It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
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.
Amino acid sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
Biological Activity
The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.
Usage
ProSpec'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.
Safety Data Sheet
Background
LIF HUMAN: Shaping the Future of Regenerative Medicine
Leukemia Inhibitory Factor, or LIF HUMAN, is a type of protein that plays a crucial role in medical and biological research. It's primarily used to maintain the growth of stem cells in a lab setting, preventing them from differentiating, which means turning into other types of cells prematurely.
The Science Behind LIF HUMAN
LIF is known for its ability to interact with certain cells in the human body, promoting or inhibiting various biological processes. For instance, it's involved in bone and fat metabolism, which helps in understanding health conditions related to these areas.
Additionally, it has a role in the development of nerve cells and affects how the immune system responds to diseases.
Production and Usage
In scientific settings, LIF is produced synthetically, often using bacteria such as Escherichia coli in factories to make it. This method allows researchers to obtain sufficient quantities of pure and functional protein for their studies.
LIF is important for researching new treatments for diseases such as leukemia because it can influence how blood cells behave.
The Benefits of Using LIF Research and Medicine
One of the key uses of LIF is in the field of stem cell research. By adding LIF to stem cell cultures, scientists can keep these cells in an undifferentiated state longer, which is vital for developing regenerative therapies. This ability has significant implications for medical treatments, offering potential advances in healing or replacing damaged tissues.
Safety and Handling
When handling LIF, especially in a research or laboratory setting, it's important to manage it with care. The protein is typically stored at very low temperatures (below -18°C) to maintain its stability and functionality over time. Researchers must also prevent it from undergoing freeze-thaw cycles, which can degrade its effectiveness.
LIF HUMAN's Impact on Health
Beyond the lab, LIF has potential therapeutic benefits. For instance, it may help in treating infertility issues by improving the implantation rates during in vitro fertilization procedures. Its influence on immune system responses also opens doors for treatments of various immune-related conditions.
Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.