Recombinant Human IL-4, Animal-Free Protein

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As an alternative, please consider our next generation Recombinant Human IL-4 (BT-004-AFL). It has equivalent bioactivity to Recombinant Human IL-4 (Catalog # AFL204). It combines R&D Systems quality with scalability ...read more

Product Details

Summary
Product Discontinued
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    • Catalog Number
      AFL204
    • Availability
      Product Discontinued

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Recombinant Human IL-4, Animal-Free Protein Summary

Details of Functionality
Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.0500-0.200 ng/mL.
The specific activity of Recombinant Human IL-4 is >1.00 x 107 IU/mg, which is calibrated against human IL-4 WHO International Standard (NIBSC code: 88/656).
Source
E. coli-derived human IL-4 protein
His25-Ser153, with an N-terminal Met
Produced using non-animal reagents in an animal-free laboratory.
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Animal-Free Recombinant Proteins
Gene
IL4
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Purity Statement
Antigen Affinity-purified
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
15 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
14 kDa, reducing conditions

Packaging, Storage & Formulations

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.
  • 12 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-4, Animal-Free Protein

  • B cell growth factor 1
  • BCDF
  • B-cell stimulatory factor 1
  • BCGF1
  • BCGF-1
  • binetrakin
  • BSF1
  • BSF-1
  • IL4
  • IL-4
  • IL-4B_cell stimulatory factor 1
  • IL4E12
  • interleukin 4
  • interleukin-4
  • Lymphocyte stimulatory factor 1
  • MGC79402
  • pitrakinra

Background

Interleukin-4 (IL-4), also known as B cell-stimulatory factor-1, is a monomeric, approximately 13 kDa‑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 nonhematopoietic 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).

  1. Benczik, M. and S.L. Gaffen (2004) Immunol. Invest. 33:109.
  2. Chomarat, P. and J. Banchereau (1998) Int. Rev. Immunol. 17:1.
  3. Yokota, T. et al. (1986) Proc. Natl. Acad. Sci. 83:5894.
  4. Redfield, C. et al. (1991) Biochemistry 30:11029.
  5. Ramirez, F. et al. (1988) J. Immunol. Meth. 221:141.
  6. Leitenberg, D. and T.L. Feldbush (1988) Cell. Immunol. 111:451.
  7. Mosman, T.R. et al. (1987) J. Immunol. 138:1813.
  8. Mueller, T.D. et al. (2002) Biochim. Biophys. Acta 1592:237.
  9. Nelms, K. et al. (1999) Annu. Rev. Immunol. 17:701.
  10. Paludan, S.R. (1998) Scand. J. Immunol. 48:459.
  11. Corthay, A. (2006) Scand. J. Immunol. 64:93.
  12. Ryan, J.J. et al. (2007) Crit. Rev. Immunol. 27:15.
  13. Grone, A. (2002) Vet. Immunol. Immunopathol. 88:1.
  14. Rosenberg, H.F. et al. (2007) J. Allergy Clin. Immunol. 119:1303.

Manufacturing Process

Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.

Production
  • All molecular biology procedures use animal-free media and dedicated labware.
  • Dedicated fermentors are utilized in committed animal-free areas.
Purification
  • Protein purification columns are animal-free.
  • Bulk proteins are filtered using animal-free filters.
  • Purified proteins are stored in animal-free containers in a dedicated cold storage room.
Quality Assurance
  • Low Endotoxin Level.
  • No impairment of biological activity.
  • High quality product obtained under stringent conditions.
  • For ex vivo research or bioproduction, additional documentation can be provided.

Please read our complete Animal-Free Statement


 

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Bioinformatics

Gene Symbol IL4
Uniprot