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Isoforms Recommended: IL-4
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IL4

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Cat. No. Compare Product Name Species Source
  • HY-P73217
    IL-4R alpha/CD124 Protein, Rat (HEK293, His)

    Interleukin-4 receptor subunit alpha; IL-4R-alpha; IL-4RA; CD124; IL4-BP; IL4R

    		 Rat HEK293
    IL-4R alpha is a subunit alpha shared by IL-4 and IL-13 receptors, found in leukocytes originally. IL-4R alpha couples to the JAK1/2/3-STAT6 pathway and involves in promoting Th2 differentiation. IL-4R alpha/CD124, Rat consists of 801 amino acids (M1-S801), exerts IL-4 binding function and results the phosphorylation of C-terminal tyrosine residues. IL-4R alpha/CD124, Rat has an immunoreceptor tyrosine inhibitor motif (ITIM) (698-703 a.a), which can bind to the SH2 domain of some phosphatases by phosphorylating ITIM. IL-4R alpha/CD124, Rat has a soluble form (1-229 a.a) and a transmembrane domain (233-256 a.a). The soluble IL-4R (sIL4R) inhibits IL4-induced spleen cell proliferation. IL-4R alpha/CD124 Protein, Rat is produced in HEK293 cells, including a Fibronectin typr III domain (125-223 a.a) and a C-Terminal His-tag.
  • HY-P74801
    IL-4R alpha/CD124 Protein, Rat (HEK293, Fc)

    Interleukin-4 receptor subunit alpha; IL4R alpha; IL4R

    		 Rat HEK293
    IL-4R alpha is a subunit alpha shared by IL-4 and IL-13 receptors, found in leukocytes originally. IL-4R alpha couples to the JAK1/2/3-STAT6 pathway and involves in promoting Th2 differentiation. IL-4R alpha/CD124, Rat consists of 801 amino acids (M1-S801), exerts IL-4 binding function and results the phosphorylation of C-terminal tyrosine residues. IL-4R alpha/CD124, Rat has an immunoreceptor tyrosine inhibitor motif (ITIM) (698-703 a.a), which can bind to the SH2 domain of some phosphatases by phosphorylating ITIM. IL-4R alpha/CD124, Rat has a a soluble form (1-229 a.a) and a transmembrane domain (233-256 a.a). The soluble IL-4R (sIL4R) inhibits IL4-induced spleen cell proliferation. IL-4R alpha/CD124, Rat is produced in HEK293 cells, including a Fibronectin typr III domain (125-223 a.a) and a C-Terminal hFc-tag.

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