Measured in a cell proliferation assay using rat splenocytes. Noble, A. and D.M. Kemery (1995) Immunology 85:357. The ED50 for this effect is 0.025-0.25 ng/mL.
Source
E. coli-derived rat IL-4 protein Cys25-Ser147, with an N-terminal Met
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
13.5 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.
Publications
Read Publications using 504-RL in the following applications:
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.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 50 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat IL-4 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). Rat IL-4 is synthesized with a 24 aa signal sequence. Mature rat IL-4 shares 41%, 43%, and 59% aa sequence identity with bovine, human, and mouse 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 IgG1 and IgE in rodent 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).
Benczik, M. and S.L. Gaffen (2004) Immunol. Invest. 33:109.
Chomarat, P. and J. Banchereau (1998) Int. Rev. Immunol. 17:1.
McKnight, A.J. et al. (1991) Eur. J. Immunol. 21:1187.
Redfield, C. et al. (1991) Biochemistry 30:11029.
Ramirez, F. et al. (1988) J. Immunol. Meth. 221:141.
Leitenberg, D. and T.L. Feldbush (1988) Cell. Immunol. 111:451.
Mosman, T.R. et al. (1987) J. Immunol. 138:1813.
Mueller, T.D. et al. (2002) Biochim. Biophys. Acta 1592:237.
Nelms, K. et al. (1999) Annu. Rev. Immunol. 17:701.
Paludan, S.R. (1998) Scand. J. Immunol. 48:459.
Corthay, A. (2006) Scand. J. Immunol. 64:93.
Ryan, J.J. et al. (2007) Crit. Rev. Immunol. 27:15.
Grone, A. (2002) Vet. Immunol. Immunopathol. 88:1.
Rosenberg, H.F. et al. (2007) J. Allergy Clin. Immunol. 119:1303.
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