IL4R Protein, Human, Recombinant (His Tag)

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IL4R Protein, Human, Recombinant (His Tag): Product Information

Purity
> 98 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its binding ability in a functional ELISA. Immobilized human IL4R-His (Cat:10402-H08H) at 10 μg/mL (100 μl/well) can bind biotinylated human IL4 (Cat:11846-HNAE). The EC50 of biotinylated human IL4 is 20.8-48.5 ng/mL.
2. Measured by its ability to inhibit IL-4 dependent proliferation of TF-1 human erthroleukemic cells. The ED50 for this effect is 4-20 ng/ml in the presence of 2 ng/ml IL-4.
Protein Construction
A DNA sequence encoding the human IL4R (NP_000409.1) precursor (Met 1-His 232) was fused with a polyhistidine tag at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Met 26
Molecule Mass
The secreted recombinant human IL4R consists of 218 amino acids after cleavage of the signal peptide and predictes a molecular mass of 25.3 kDa. In SDS-PAGE under reducing conditions, it migrates with the apparent molecular mass of 43-48 kDa due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

IL4R Protein, Human, Recombinant (His Tag): Images

Measured by its ability to inhibit IL-4 dependent proliferation of TF-1 human erthroleukemic cells. The ED50 for this effect is 4-20 ng/ml in the presence of 2 ng/ml IL-4.

IL4R Protein, Human, Recombinant (His Tag): Alternative Names

CD124 Protein, Human; IL-4RA Protein, Human; IL4R Protein, Human; IL4RA Protein, Human

IL4R Background Information

The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 32 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD124, also known as interleukin 4 receptor (IL4R), is a typeⅠ transmembrane protein that can regulate IgE antibody production in B cells through binding to interleukin 4 and interleukin 13 and promote differentiation of Th2 cells through binding to interleukin 4. The membrane-bound form of CD124 can be hydrolyzed to soluble form which can inhibit IL4-mediated cell proliferation and IL5 upregulation by T-cells.
Full Name
interleukin 4 receptor
References
  • Zola H, et al. (2007) CD molecules 2006-human cell differentiation molecules. J Immunol Methods. 318 (1-2): 1-5.
  • Ho IC, et al. (2009) GATA3 and the T-cell lineage: essential functions before and after T-helper-2-cell differentiation. Nat Rev Immunol. 9 (2): 125-35.
  • Matesanz-Isabel J, et al. (2011) New B-cell CD molecules. Immunology Letters.134 (2): 104-12.
  • Construction and Application of Elastin Like Polypeptide Containing IL-4 Receptor Targeting Peptide
    Author
    Sarangthem, V;Cho, EA;Bae, SM;Singh, TD;Kim, SJ;Kim, S;Jeon, WB;Lee, BH;Park, RW;
    Year
    2013
    Journal
    PLoS ONE
    Application
    SPR
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