LIF Human, Yeast
LIF Human Recombinant, Yeast
Cat. No.
BT19374
Source
Pichia pastoris.
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.
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Description
LIF Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 58.5 kDa. The LIF is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Leukemia Inhibitory Factor (LIF) is a lymphoid factor that plays a crucial role in maintaining embryonic stem cells in their undifferentiated state by preventing spontaneous differentiation. LIF exhibits various functions, including promoting the differentiation of cholinergic neurons, regulating stem cell pluripotency, influencing bone and fat metabolism, stimulating the growth of factor-dependent cell lines, and enhancing the production of megakaryocytes in living organisms. Notably, there is a high degree of similarity between human and mouse LIF, with 78% identical amino acid sequences.
Description
Recombinant Human LIF, produced in yeast, is a single-chain polypeptide that has undergone glycosylation. It comprises 180 amino acids and has a molecular weight of 58.5 kDa. The purification process for LIF involves specialized chromatographic techniques.
Physical Appearance
White, lyophilized (freeze-dried) powder that has been sterilized by filtration.
Formulation
The protein was lyophilized from a 0.2 μm filtered phosphate-buffered saline (PBS) solution.
Solubility
To reconstitute the lyophilized LIF, it is advised to dissolve it in sterile, 18 megaohm-centimeter (MΩ·cm) H₂O at a concentration of at least 100 μg/mL. This solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized LIF remains stable for up to 3 weeks at room temperature. However, for long-term storage, it is recommended to store the desiccated product at temperatures below -18°C. Once reconstituted, LIF can be stored at 4°C for 2-7 days. For longer storage periods, it should be kept at temperatures below -18°C. It is crucial to avoid repeated freeze-thaw cycles to maintain protein stability.
Purity
The purity of the protein is greater than 98.0%, as determined by the following methods: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis, and (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity of recombinant human LIF was evaluated based on its ability to induce the differentiation of murine M1 myeloid leukemia cells. The minimum concentration of human LIF required to elicit a detectable response in this assay is less than 0.05 ng/mL. The specific activity of the protein is greater than 1 x 10⁸ units/mg.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Source
Pichia pastoris.
Amino Acid Sequence
S P L P I T P V N A T C A I R H P C H N N L M N Q I R S Q L A Q L N G S A N A L F I L Y Y T A Q G E P F P N N L D K L C G P N V T D F P P F H A N G T E K A K L V E L Y R I V V Y L G T S L G N I T R D Q K I L N P S A L S L H S K L N A T A D I L R G L L S N V L C R L C S K Y H V G H V D V T Y G P D T S G K D V F Q K K K L G C Q L L G K Y K Q I I A V L A Q A F.
Product Science Overview
Production and Characteristics
Human Recombinant LIF produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and has a molecular mass of approximately 58.5 kDa . The expression host for this recombinant protein is typically Pichia pastoris, a species of yeast known for its ability to perform post-translational modifications similar to those in higher eukaryotes .
The recombinant LIF is purified using proprietary chromatographic techniques to ensure high purity, typically greater than 98% as determined by RP-HPLC and SDS-PAGE . The protein is lyophilized from a 0.2 µm filtered PBS solution and is recommended to be reconstituted in sterile water to a concentration of at least 100 µg/ml .
Biological Functions
LIF has several important biological functions, including:
- Maintenance of Embryonic Stem Cells: LIF is crucial for the long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation .
- Neuronal Differentiation: It promotes the differentiation of cholinergic neurons .
- Bone and Fat Metabolism: LIF plays a role in the regulation of bone and fat metabolism .
- Hematopoiesis: It is involved in the mitogenesis of factor-dependent cell lines and the promotion of megakaryocyte production in vivo .
- Inflammation: LIF has a role in inflammatory responses .
Applications
Recombinant human LIF is widely used in research and biotechnology for various applications, including:
- Stem Cell Research: LIF is used to maintain the pluripotency of embryonic stem cells and induced pluripotent stem cells (iPSCs) in culture .
- Differentiation Studies: It is employed in studies investigating the differentiation of various cell types .
- Functional Assays: LIF is used in functional assays to study its effects on different biological processes .
Stability and Storage
Lyophilized LIF is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage . Upon reconstitution, it should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use. It is important to avoid freeze-thaw cycles to maintain the protein’s stability .
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