Name :
Recombinant Canine IL-4 Protein

Biological Activity :

Background :
Interleukin-4, also known as IL4, is a secreted protein that belongs to the IL-4 / IL-13 family. Interleukin-4 / IL4 has many biological roles, including the stimulation of activated B-cell and T-cell proliferation. It enhances both secretion and cell surface expression of IgE and IgG1. Interleukin-4 / IL4 also regulates the expression of the low-affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Interleukin-4 is essential for the switching of B cells to IgE antibody production and the maturation of T helper (Th) cells toward the Th2 phenotype. It participates in at least several B-cell activation processes as well as other cell types. However, studies show that double mutant (Q116D, Y119D) of the murine IL4 protein (QY), both glutamine 116 and tyrosine 119, which binds to the IL4 receptor alpha, completely inhibits in a dose-dependent manner the IL4-induced proliferation of lipopolysaccharide-stimulated murine splenic B-cells, of the murine T cell line CTLL-2, and the murine pre-B-cell line BA/F3. QY also inhibited the IL4-stimulated up-regulation of CD23 expression by lipopolysaccharide-stimulated murine splenic B-cells and abolished tyrosine phosphorylation of the transcription factor Stat6 and the tyrosine kinase Jak3 in IL4-stimulated BA/F3 cells. Cancer Immunotherapy Immune Checkpoint Immunotherapy Targeted Therapy

Biological Activity :
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells.The ED50 for this effect is typically 5-30 ng/ml.

Expression Host :
Canine

Source :
E. coli

Tag :

Protein Accession No. :
O77762

NCBI Gene ID :

Synonyms :

Synonyms :
interleukin 4

Amino Acid Sequence :

Molecular Weight :
The recombinant canine IL4 consists of 109 amino acids and has a calculated molecular mass of 13 kDa. In SDS-PAGE under reducing conditions, it migrates as an approximately 12-14 KDa band.

Purity :
> 96 % as determined by SDS-PAGE

State of Matter :

Product Concentration :

Storage and Stability :
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.

Endotoxin Level :
Please contact us for more information.

Protein Construction :
A DNA sequence encoding the canine IL4 (O77762) (His 25-His 132) was expressed, with an initial Met at the N-terminus.

Buffer Solution :
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 hardcopy of datasheet.

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.

Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Synonyms :

References & Citations :
Grunewald SM. et al., 1998, J Immunol. 160 (8): 4004-9. Susanne M. et al, 1997, THE JOURNAL OF BIOLOGICAL CHEMISTRY. 272 (3): 1480-3. Nishikubo K. et al., 2003, Gene Ther. 10 (26): 2119-25.

MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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