|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A polyhistidine-tag is an amino acid motif in proteins that consists of at least five histidine (His) residues, often at the N- or C-terminus of the protein.
Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems.
|Canine IL4 ORF mammalian expression plasmid, C-GFPSpark tag||DG70021-ACG|
|Canine IL4 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||DG70021-ACR|
|Canine IL4 ORF mammalian expression plasmid, C-Flag tag||DG70021-CF|
|Canine IL4 ORF mammalian expression plasmid, C-His tag||DG70021-CH|
|Canine IL4 ORF mammalian expression plasmid, C-Myc tag||DG70021-CM|
|Canine IL4 ORF mammalian expression plasmid, C-HA tag||DG70021-CY|
|Canine IL4 Gene cDNA clone plasmid||DG70021-G|
|Canine IL4 ORF mammalian expression plasmid, N-Flag tag||DG70021-NF|
|Canine IL4 ORF mammalian expression plasmid, N-His tag||DG70021-NH|
|Canine IL4 ORF mammalian expression plasmid, N-Myc tag||DG70021-NM|
|Canine IL4 ORF mammalian expression plasmid, N-HA tag||DG70021-NY|
|Canine IL4 natural ORF mammalian expression plasmid||DG70021-UT|
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Interleukin-4, also known as IL4, is a secreted protein which 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 for the maturation of T helper (Th) cells toward the Th2 phenotype. It participates in at least several B-cell activation processes as well as of 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 inhibites 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 of 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.