Recombinant Human IL-4 GMP Protein, CF

Animal-Free.
  
  • Purity
    >97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    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 0.05-0.2 ng/mL.
    The specific activity of recombinant human IL-4 is approximately 2.9 x 104 IU/μg, which is calibrated against human IL-4 WHO International Standard (NIBSC code: 88/656).
  • Source
    E. coli-derived His25-Ser153, with an N-terminal Met Produced using non-animal reagents in an animal-free laboratory.
    Manufactured and tested under cGMP guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis
    Met-His25-Lys-(Cys)-Asp-Ile-Thr-Leu-Gln-Glu
  • Predicted Molecular Mass
    15.1 kDa
  • SDS-PAGE
    14 kDa, reducing conditions
204-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100-200 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Data Images
GMP-grade Recombinant Human IL‑4 (Catalog # 204‑GMP) stimulates proliferation of TF‑1 human erythroleukemic cells. The ED50 is 0.05‑0.2 ng/mL.
1 μg/lane of GMP-grade Recombinant Human IL-4 (Catalog # 204-GMP) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 14 kDa.
Mass Spectrometry
MALDI-TOF analysis of GMP-grade Recombinant Human IL-4 (Catalog # 204-GMP). The major peak at 15083 Da corresponds to the calculated molecular mass, 15094 Da. The minor peak at 15297 Da is a matrix-associated artifact of the MALDI-TOF.
Background: IL-4

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).

  • References:
    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.
  • Long Name:
    Interleukin 4
  • Entrez Gene IDs:
    3565 (Human); 16189 (Mouse); 287287 (Rat); 397225 (Porcine); 280824 (Bovine); 403785 (Canine); 574281 (Primate); 100302454 (Rabbit)
  • Alternate Names:
    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; interleukin 4; interleukin-4; Lymphocyte stimulatory factor 1; MGC79402; pitrakinra

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