GMP IL-4 Protein, Human

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. GMP IL-4 Protein, Human 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.

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells and the ED₅₀ for this effect is 0.05-0.2 ng/mL.

Human

E. coli

Tag Free

P05112-1 (H25-S153)

3565  [NCBI]

Full Length of Isoform-1 Mature Protein

HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS

Approximately 15 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.22 μm filtered solution of 50 mM Tris, 300 mM NaCl, pH 7.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<0.01 EU/μg, determined by LAL method.

N/A.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.