LIF Human

Leukemia Inhibitory Factor Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT19022
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

LIF Human, GST

Leukemia Inhibitory Factor, GST tag Human Recombinant

LIF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (23-202a.a.) and having a molecular mass of 47.2kDa.
LIF is fused to a 236 amino acid His-GST tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19110
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

LIF Human, His

Leukemia Inhibitory Factor Human Recombinant, His tag

LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).

Shipped with Ice Packs
Cat. No.
BT19199
Source

Escherichia Coli.

Appearance
Filtered White lyophilized (freeze-dried) powder.

LIF Human, Sf9

Leukemia Inhibitory Factor Human Recombinant, Sf9

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.

Shipped with Ice Packs
Cat. No.
BT19290
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

LIF Human, Yeast

LIF Human Recombinant, Yeast

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.
Shipped with Ice Packs
Cat. No.
BT19374
Source
Pichia pastoris.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

LIF Mouse

Leukemia Inhibitory Factor Mouse Recombinant

Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.
The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19449
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

LIF Rat

Leukemia Inhibitory Factor Rat Recombinant

Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19534
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

LIFR Human

Leukemia Inhibitory Factor Receptor Alpha Human Recombinant

LIFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 798 amino acids (45-833a.a.) and having a molecular mass of 90.5kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).
LIFR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19779
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

LIFR Mouse

Leukemia Inhibitory Factor Receptor Alpha Mouse Recombinant

LIFR Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 794 amino acids (44-828 aa) and having a molecular mass of 89.6kDa.
LIFR is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT19854
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.
Definition and Classification

Leukemia Inhibitory Factor (LIF) is a cytokine belonging to the interleukin-6 (IL-6) family. It is known for its ability to inhibit the differentiation of myeloid leukemic cells, hence its name . LIF is classified as a polyfunctional glycoprotein cytokine that can affect various cell types and tissues .

Biological Properties

LIF exhibits several key biological properties:

  • Expression Patterns: LIF is expressed in various tissues, including the trophectoderm of developing embryos .
  • Tissue Distribution: It is found in multiple tissues such as bone, neural tissues, and the reproductive system .
  • Key Properties: LIF influences cell growth, differentiation, and survival. It plays roles in bone metabolism, neural development, embryogenesis, and inflammation .
Biological Functions

LIF has diverse biological functions:

  • Primary Functions: It induces the terminal differentiation of myeloid leukemic cells, preventing their proliferation . It also promotes the growth and differentiation of various target cells .
  • Role in Immune Responses: LIF is involved in immune responses by modulating the activity of macrophages and other immune cells .
  • Pathogen Recognition: It plays a role in recognizing and responding to pathogens by influencing immune cell behavior .
Modes of Action

LIF operates through several mechanisms:

  • Binding Partners: LIF binds to the LIF receptor (LIFR), which forms a heterodimer with the gp130 receptor .
  • Downstream Signaling Cascades: This binding activates multiple signaling pathways, including JAK/STAT, MAPK, and PI3K pathways . These cascades lead to changes in gene expression and cellular responses .
Regulatory Mechanisms

The expression and activity of LIF are tightly regulated:

  • Transcriptional Regulation: LIF expression is controlled at the transcriptional level by various factors .
  • Post-Translational Modifications: LIF undergoes glycosylation, which affects its stability and activity . Additionally, its signaling is modulated by proteins such as SOCS (suppressors of cytokine signaling) and PIAS (protein inhibitors of activated STAT) .
Applications

LIF has several applications in biomedical research and therapy:

  • Biomedical Research: It is used in stem cell research to maintain the pluripotency of embryonic stem cells .
  • Diagnostic Tools: LIF can serve as a biomarker for certain cancers, such as pancreatic cancer .
  • Therapeutic Strategies: LIF has potential therapeutic applications in treating infertility, cancer, and tissue regeneration .
Role in the Life Cycle

LIF plays crucial roles throughout the life cycle:

  • Development: It is essential for embryo implantation and early development .
  • Aging and Disease: LIF is involved in tissue regeneration and repair, making it relevant in aging and disease contexts . It also plays roles in neurogenesis and immune responses throughout life .
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