I17003 Sigma

Interleukin-4 human

IL-4, recombinant, expressed in HEK 293 cells, cell culture tested, endotoxin tested

Synonym: IL-4, Interleukin-4 human



recombinant   expressed in HEK 293 cells
assay   ≥98% (SDS-PAGE)
potency   ≤1 ng/mL ED50
mol wt   mol wt 14.9 kDa ((glycosylated))
suitability   cell culture tested
  endotoxin tested
storage temp.   −20°C


Analysis Note

The biological activity of recombinant human IL-4 was tested in culture by measuring its ability to stimulate proliferation of human TF-1 cells (human erythroleukemic indicator cell line).

Physical form

Supplied as a lyophilized powder containing phosphate buffered saline.

Biochem/physiol Actions

IL-4 is a protein that has been shown to regulate a wide spectrum of functions in B cells, T cells, monocytes/macrophages and other haematopoietic and non-haematopoietic cells. Among T cell clones, IL-4 is produced by Th0 and Th2 cells, but not Th1 cells, and this has now been demonstrated both in mice and in humans. IL-4 blocks the production of proinflammatory cytokines such IL-6, TNFα, and M-CSF and improves the differentiation of immature DCs from CD34+ progenitors when added during the differentiation period (day 6 to day 12).

Interleukin-4 is a lymphokine with profound effects on the growth and differentiation of immunologically competent cells. IL-4 is also known as B cell stimulatory factor-1 (BSF-1), T cell growth factor-2 (TCGF-2) and mast-cell growth factor-2 (MCGF-2). Inhibits VEGF-induced and bFGF-induced angiogenesis. IL-4 is a complex glycoprotein released by a subset of activated T cells. Human and mouse IL-4 share 50% amino acid sequence homology, but their biological actions are species-specific.

General description

Recombinant human Interleukin-4 (IL-4) is expressed in human 293 cells as a glycoprotein with a calculated moleculaer mass of 14.9 kDa. This protein is manufactured in human cells using an all-human production system, with full chemically defined ingredients and with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports better stability of the protein in culture.



Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 
Protocols & Articles
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