- 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.
Safety Data Sheet
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.
Background
A cytokine that is part of the interleukin 6 family, Leukaemia inhibitory factor or LIF operates in the hypothalamus. Studies have shown that it may play a crucial role in energy homeostasis. The cytokine has also been found in the anterior pituitary and is able to trigger ACTH secretion in vitro and vivo, shown in studies on both mice and men. Indeed, studies have shown low plasma ACTH and damage HPA responses to immune stimuli or stress can both be corrected by LIF administration.
Function
LIF gets its name from its power to induce terminal differentiation of myeloid leukemia cells. What this means is that LIF prevents their growth from continuing. You will also find certain other factors attributed to LIF such as influence on bone metabolism, embryogenesis, inflammation, and the growth promotion, as well as the differentiation of different groups of target cells. It is believed by some that LIF could help to improve the implantation rate in women who have experienced unexplained infertility.
LIF has also been shown and indeed suggested as a possible alternate solution to feed cell culture. This is due to the limit that feeder cells actually only create LIF on the surface of the cells. Feeder cells that do not produce the LIF gene have been found not to effectively support stem cells. In contrast, LIF can effectively ensure self renewal. It is able to do this by gaining the activator of Stat3 and the signal transducer. Typically, LIF will be added to stem cell culture with the aim of reducing the chances of spontaneous differentiation.
Structure
The structure of LIF is made of main chain fold that conforms to the four a-helix bundle topology. This has been seen in various other members of the hematopoietic cytokine family. LIF is quite similar in terms of structure to both GH and granulocyte colony-stimulating factor. Studies and x-rays have also shown evidence for regions of conserved surface character.
Interactions
Over the years, studies have shown that LIF interacts with various other factors including the ciliary neurotrophic factor. The two share various common components through their multimeric receptors. The two cytokine receptors both contain gp190/low affinity LIF receptor and gp130/interleukin-60receptor transducer. Research has shown a mutual displacement toward the trimeric high-affinity CNTF receptor for LIF and CNTF. One study suggested that competition between the two factors is a result of three receptor components to establish a conformational site that is apparent for both LIF and CNTF.
Mechanisms
When LIF binds to the LIF receptor also known as LIFR-a, a heterodimer is formed. This has a specific subunit and that is apparent for all members of this particularly receptor family. The formation of the heterodimer than leads to the activation of JAK/STAT as well as MAPK.
Typically, LIFe will be expressed in the trophectoderm of an embryo developing. The receptor, LIFR, is then expressed through the inner cell mass. Embryonic stem cells come from the inner cell mass during the blastocyst stage. As such, once they are removed, this also removes the LIF source.