IL-4 Protein, Human (Biotinylated)

The IL-4 protein is primarily secreted by mast cells, T cells, eosinophils, and basophils and is critical for antibody production, hematopoiesis, and immune responses. It induces MHC class II expression on B cells, enhances IgE and IgG1 secretion, and modulates CD23 and IL31RA expression. IL-4 Protein, Human (Biotinylated) is the recombinant human-derived IL-4 protein, expressed by E. coli , with tag free.

The cytokine IL-4, primarily secreted by mast cells, T-cells, eosinophils, and basophils, plays a crucial role in regulating antibody production, hematopoiesis, inflammation, and the development of effector T-cell responses. IL-4 induces the expression of class II MHC molecules on resting B-cells and enhances both the secretion and cell surface expression of IgE and IgG1, contributing to immune responses. Additionally, IL-4 regulates the expression of the low-affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes and positively regulates IL31RA expression in macrophages. Furthermore, IL-4 stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and inducing RUFY4. Beyond its immunological functions, IL-4 plays a critical role in higher functions of the normal brain, such as memory and learning. Upon binding to its receptor, IL-4R, IL-4 initiates signaling through two types of receptor complexes, type 1 mainly on hematopoietic cells and type 2 on nonhematopoietic cells, activating JAK3 and to a lesser extent JAK1 phosphorylation, leading to the activation of the signal transducer and activator of transcription 6/STAT6. IL-4 interacts with both IL-4R and IL13RA1 to mediate its diverse physiological effects.

Human

E. coli

Tag Free

P05112-1 (H25-S153)

3565  [NCBI]

Approximately 60.4 kDa.

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.