SKU: PR00215 Category:

Recombinant Mouse IL4 Protein, C-His

$999.00

SKU: PR00215
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Product details

Background:
Interleukin-4 (IL-4) is a pleiotropic cytokine that regulates diverse T and B cell responses including cell proliferation, survival and gene expression. IL-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of naive CD4+ T cells into helper Th2 cells, characterized by their cytokine-secretion profile that includes secretion of IL-4, IL-5, IL-6, IL-10, and IL-13, which favor a humoral immune response. Another dominant function of IL-4 is the regulation of immunoglobulin class switching to the IgG1 and IgE isotypes. Excessive IL-4 production by Th2 cells has been associated with elevated IgE production and allergic response.

Specifications

Size10μg/50μg/500μg/1mg
SpeciesMouse
SourceHuman Cells
TagC-6His
Accession NumberP07750
KnownAsInterleukin-4; IL-4; IL4; B-cell IgG differentiation factor; B-cell growth factor 1; B-cell stimulatory factor 1; BSF-1; IGG1 induction factor; Lymphocyte stimulatory factor 1
Protein LengthHis21-Ser140
Predicted Mol Mass14.6 KDa
N-terminal Sequence
SDS-PAGE15-22 KDa, reducing conditions
Endotoxin< 1 EU/µg as determined by LAL test.
FormulationLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Purity-SDS-PAGE>95% as determined by SDS-PAGE.
BioactivityMeasured in a cell proliferation assay using M-NFS-60 mouse lymphoblast cells. The ED50 for this effect is 43.59pg/ml. (Regularly tested)
ShippingLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
StorageThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
ReconstitutionAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
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Question:

How does the activity of your recombinant proteins compare to competitors?

Wenjng
24-Jul-2025

Answer:

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

Question:

What is the specific activity or ED50 of my recombinant protein?

Wenjng
24-Jul-2025

Answer:

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Question:

Have your recombinants been tested for stability?

Wenjng
24-Jul-2025

Answer:

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Question:

Does specific activity of a recombinant protein vary between lots?

Wenjng
24-Jul-2025

Answer:

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

Question:

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Wenjng
24-Jul-2025

Answer:

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Question:

Why is protein freeze-dried? What is the effect of freeze-drying on protein?

Wenjng
24-Jul-2025

Answer:

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.

Question:

What is the general protectant? What kind of protectant do you usually add?

Wenjng
24-Jul-2025

Answer:

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.

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