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Your Position: Home > Protein > IL-4 > IL4-H82E0

Biotinylated Human IL-4 Protein, Avitag™,His Tag (MALS verified)

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  • Synonym
    IL4,BCGF1,BSF1
  • Source
    Biotinylated Human IL-4, Avitag,His Tag(IL4-H82E0) is expressed from human 293 cells (HEK293). It contains AA His 25 - Ser 153 (Accession # AAH67514).
    Predicted N-terminus: His 25
  • Molecular Characterization
    IL-4 Structure

    This protein carries an Avi tag (Avitag™) at the C-terminus, followed by a polyhistidine tag

    The protein has a calculated MW of 17.6 kDa. The protein migrates as 22 kDa under reducing (R) condition, and 21 kDa under non-reducing (NR) condition (SDS-PAGE) due to glycosylation.

  • Labeling
    Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
  • Protein Ratio
    Passed as determined by the HABA assay / binding ELISA.
  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
IL-4 SDS-PAGE

Biotinylated Human IL-4, Avitag,His Tag on SDS-PAGE under reducing (R) and non-reducing (NR) conditions. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

SEC-MALS
IL-4 MALS images

The purity of Biotinylated Human IL-4, Avitag,His Tag (Cat. No. IL4-H82E0) is more than 85% and the molecular weight of this protein is around 18-25 kDa verified by SEC-MALS.

Bioactivity-ELISA
 IL-4 ELISA

Immobilized Human IL-4 R alpha, His Tag (Cat. No. ILR-H5221) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IL-4, Avitag,His Tag (Cat. No. IL4-H82E0) with a linear range of 2-16 ng/mL (QC tested).

 IL-4 ELISA

Immobilized Human IL-4 R alpha, Fc Tag (Cat. No. ILR-H5253) at 5 μg/mL (100 μL/well)can bind Biotinylated Human IL-4, Avitag,His Tag (Cat. No. IL4-H82E0) with a linear range of 0.1-2 ng/mL (Routinely tested).

 IL-4 ELISA

Serial dilutions of Monoclonal IL-4R/CD124 Neutralizing Antibody were added into Human IL-4 R alpha, His Tag (Cat. No. ILR-H5221): Biotinylated Human IL-4, Avitag,His Tag (Cat. No. IL4-H82E0) binding reactions. The half maximal inhibitory concentration (IC50) is 0.505 μg/mL (Routinely tested).

Bioactivity-Bioactivity CELL BASE
 IL-4 CELL

Biotinylated Human IL-4, Avitag,His Tag (Cat. No. IL4-H82E0) stimulates the proliferation of TF-1 human erythroleukemic cells. The ED50 for this effect is 1.19-2.64 ng/mL (Routinely tested).

  • Background
    Interleukin-4, is a cytokine that induces differentiation of naive helper T cells (Th0 cells to Th2 cells). In the presence of IL-4 and IL-13, cytokines that are produced in a Th-2 type response, particularly during allergy and parasitic infections, macrophages become differentially activated, And this cytokine is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. Recently, researcher found that the cytokine IL-4 plays a key role in development of innate CD8+ T cells in the thymus of several gene-deficient mouse strains, including Itk, KLF2, CBP and Id3, without previous exposure to antigen.
  • Clinical and Translational Updates

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