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Recombinant Mouse IL13

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Product Source Size Cat. No. Price
Recombinant Mouse IL13 E. coli10 µg Z200245 $70.00
100 µg Z200247 $350.00
1.0 mg Z200249 $1,890.00
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Data Sheet
Print Version
Alternative Names IL-13, T-cell activation protein P600
Recombinant Mouse Interleukin-13 (IL13)
Description Mouse IL-13 is produced primarily by activated Th2 cells. Human IL-13 is expressed in activated T helper cells (resembling Th0, Th1, Th2), and T cells expressing CD8. The alpha chain of the IL-13 receptor has weak binding activity for IL-13. High affinity receptors are formed when the receptor alpha chains of IL-13 and IL-4 receptors are coexpressed. The receptors for IL-13 and IL-4 share a component, a common gamma subunit that is found also in the IL-2 receptor. Different IL-13 receptor structures have been shown to exist on various cell types and the IL-13 receptor may share more than one component with IL-4 receptor. IL-13 down-modulates macrophage activity, reducing the production of pro-inflammatory cytokines and chemokines in response to IFN-gamma or bacterial lypopolysaccharides. IL-13 enhances the production of the IL-1 receptor antagonist IL-1ra. IL-13 also decreases the production of nitric oxide by activated macrophages, leading to a decrease in parasiticidal activity. IL-13 induces differentiation of human monocytes, enhances survival time in culture, and also induces differentiation and proliferation and isotype switching in B cells.
Gene Symbol IL13
Gene ID 16163
Accession No. P20109
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 12.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Gel Image Click To Enlarge
Bioactivity The ED(50) was determined by the dose-dependent proliferation of TF-1 cells was ≤ 2.0 ng/mL, corresponding to a specific activity of ≥ 1.0 x 10^6 units/mg.
Bioactivity Data Click To Enlarge
Formulation Recombinant mouse IL-13 was lyophilized from a 0.2 μm filtered PBS solution.
Reconstitution A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
FAQs
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How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.

· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).

· For recombinant proteins: EU is reported per microgram of protein.

· One EU = 0.1-0.2 ng endotoxin/µg of protein.

· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.