Recombinant Canine IL4 Protein

Name: Recombinant Canine IL4 Protein
Brand: Beta LifeScience
SKU: BLPSN-2899
Availability: InStock

Collections: Cytokines and growth factors, Interleukins and receptors, Recombinant interleukin-4 (il-4) proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Canine
Accession	O77762
Background	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.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description	A DNA sequence encoding the canine IL4 (O77762) (His 25-His 132) was expressed, with an initial Met at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	His 25-His 132
Molecular Weight	The recombinant canine IL4 consists of 109 a.a. 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
Endotoxin	Please contact us for more information.
Bioactivity	Measured in a cell proliferation assay using TF-1 human erythroleukemic cells.The ED50 for this effect is typically 5-30 ng/ml.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
Subcellular Location	Secreted.
Protein Families	IL-4/IL-13 family
Database References	KEGG: cfa:403785 STRING: 9615.ENSCAFP00000001253 UniGene: Cfa.39

Gene Functions References

immunoreactivities of inflammatory cytokines, such as interleukin (IL)-2, its receptor (IL-2R), IL-4 and its receptor (IL-4R) in the cervical and lumbar spinal cord of young adult and aged beagle dogs, were compared. PMID: 23605681
In dogs with leishmaniasis, there was high expression of genes encoding IL-4 in blood leucocytes. The predominance of IL-4 gene expression in the blood of asymptomatic dogs may favour parasite replication. PMID: 21511273
The anti-inflammatory and anabolic effects of regulated expression of IL-4 in chondrocyte-scaffolds under in vitro inflammatory conditions, were investigated. PMID: 21991344
This study focuses on the co-expression of interleukin-4 (IL-4) and insulin-like-growth factor-1 (IGF-1), which specifically target inflammation and cartilage repair, respectively. PMID: 20188584
These findings suggest that polyunsaturated fatty acids are able to influence proliferation of peripheral blood mononuclear cells in healthy and atopic dogs but do not seem to influence cytokine transcription. PMID: 20187917
IL-4 expressed in canine articular chondrocytes is biologically active and suppresses inflammatory mediators in vitro. PMID: 18789870

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.