Detects human IL-4 in Western blots. In Western blots, no cross-reactivity with recombinant mouse IL‑4, recombinant porcine IL‑4, recombinant cotton rat IL‑4, recombinant rat IL‑4, or recombinant human IL‑13 is observed.
Monoclonal Mouse IgG2B Clone # 34019
Protein A or G purified from hybridoma culture supernatant
E. coli-derived recombinant human IL‑4 His25-Ser153 Accession # P05112
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize IL‑4-induced proliferation in the TF‑1 human erythroleukemic cell line. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The Neutralization Dose (ND50) is typically 0.5-1.5 µg/mL in the presence of 0.5 ng/mL Recombinant Human IL‑4.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Cell Proliferation Induced by IL‑4 and Neutralization by Human IL‑4 Antibody. Recombinant Human IL‑4 (Catalog # 204-IL) stimulates proliferation in the TF‑1 human erythroleukemic cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human IL‑4 (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human IL‑4 Monoclonal Antibody (Catalog # MAB204). The ND50 is typically 0.5-1.5 µg/mL.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Interleukin-4 (IL-4), also known as B cell-stimulatory factor-1, is a monomeric, approximately 13-18 kDa Th2 cytokine that shows pleiotropic effects during immune responses (1‑3). It is a glycosylated polypeptide that contains three intrachain disulfide bridges and adopts a bundled four alpha -helix structure (4). Human IL-4 is synthesized with a 24 aa signal sequence. Alternate splicing generates an isoform with a 16 aa internal deletion. Mature human IL-4 shares 55%, 39%, and 43% aa sequence identity with bovine, mouse, and rat IL-4, respectively. Human, mouse, and rat IL-4 are species-specific in their activities (5-7). IL-4 exerts its effects through two receptor complexes (8, 9). The type I receptor, which is expressed on hematopoietic cells, is a heterodimer of the ligand binding IL-4 R alpha and the common gamma chain (a shared subunit of the receptors for IL-2, -7, -9, -15, and -21). The type II receptor on non-hematopoietic cells consists of IL-4 R alpha and IL-13 R alpha 1. The type II receptor also transduces IL-13 mediated signals. IL-4 is primarily expressed by Th2-biased CD4+ T cells, mast cells, basophils, and eosinophils (1, 2). It promotes cell proliferation, survival, and immunoglobulin class switch to IgG4 and IgE in human B cells, acquisition of the Th2 phenotype by naïve CD4+ T cells, priming and chemotaxis of mast cells, eosinophils, and basophils, and the proliferation and activation of epithelial cells (10-13). IL-4 plays a dominant role in the development of allergic inflammation and asthma (12, 14).
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R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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