| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Leukemia inhibitory factor|LIF|Differentiation-stimulating factor|D factor|Melanoma-derived LPL inhibitor|MLPLI|LIF|HILDA |
| Assay Time | |
| Detection Method | |
| Detection Range | |
| Product Type | |
| Reactivity | |
| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
| Sensitivity | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Background
porcine LIF (Leukemia Inhibitory Factor) is a molecular target commonly studied in signal transduction, immunology, and developmental biology research. Many proteins are studied as molecular readouts that can change with cellular state, tissue remodeling, or stress responses.
Biological role and mechanism
The biological role of LIF is typically understood in terms of its molecular category and interaction network. Depending on the model system, it may participate in cell–cell communication, intracellular signaling, enzymatic processing, or regulation of gene expression programs. Mechanistic interpretation is often strengthened by considering upstream regulators and downstream readouts rather than relying on a single marker.
Expression and abundance of LIF can vary by tissue, cell type, and physiological state. In many systems, levels are influenced by factors such as developmental stage, immune activation, metabolic status, and cellular stress. Because sample matrix and pre-analytical handling can affect measured concentrations, interpretation is typically strongest when experiments keep collection and processing consistent across groups.
Nomenclature and related terms
LIF (Leukemia Inhibitory Factor) may also be referenced as Leukemia inhibitory factor, LIF, and Differentiation-stimulating factor in the literature or in databases. When comparing results across studies, confirm that the reported analyte refers to the same molecule, species context, and molecular form (e.g., precursor vs mature protein, or soluble vs membrane-associated forms).
Why it matters in research
- Understanding how LIF relates to innate and adaptive immune responses, cytokine signaling networks, host–pathogen interactions, and immune cell activation and trafficking in signal transduction, immunology, and developmental biology research.
- Interpreting shifts in LIF levels alongside other pathway components or complementary markers.
- Connecting molecular changes to phenotypes such as inflammation, remodeling, metabolism shifts, or cell-state transitions (context-dependent).
Molecular forms and interpretation
For some targets, isoforms, proteolytic processing, or post-translational modifications (such as phosphorylation or glycosylation) can influence function and apparent abundance. If multiple molecular forms are expected in your model, align interpretation with the form most relevant to the biological question.
Disease and translational relevance
LIF has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with signal transduction, immunology, and developmental biology studies. These associations are interpreted as research findings rather than diagnostic or therapeutic claims, and they should be evaluated alongside model-specific covariates and study design.
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Chemerin affects the cytokine production and the expression of their receptors in the porcine endometrium during early pregnancy and the estrous cycle: an in vitro study
IF: 3.1 Journal: Biology of Reproduction Author: Department of Animal Anatomy and Physiology, Faculty of Biology and Biotechnology, University of Warmia and Mazury in Olsztyn, Olsztyn, Poland. Cited Date: 2024-09-27
PPAR gamma ligands regulate the expression of inflammatory mediators in porcine endometrium during LPS-induced inflammation
IF: 2.74 Journal: Theriogenology Cited Date: 2022-05-06
PPARγ ligands modulate the immune response mediators in the pig myometrium—an in vitro study
IF: 2.145 Journal: Animal Reproduction Science Cited Date: 2021-10-09