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Recombinant Mouse IL5

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Product Source Size Cat. No. Price
Recombinant Mouse IL5 Insect cells 25 µg Z200475 $600.00
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Data Sheet
Print Version
Alternative Names IL-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, TRF
Recombinant Mouse Interleukin-5 (IL5)
Description Interleukin-5 is a specific hematopoietic growth factor that is responsible for the growth and differentiation of eosinophils. IL-5 promotes the growth of immature hematopoietic progenitor cells BFU-E while it causes differentiation of CFU-E the proliferation of which is inhibited by IL-5. IL-5 strongly stimulates the proliferation, cell activation, and differentiation of eosinophils. B cells can be made responsive to IL-5 by treatment with suboptimal doses of IL-1. Interleukin-5 also promotes the generation of cytotoxic T cells from thymocytes. In thymocytes IL-5 induces the expression of high affinity IL-2 receptors. In contrast to human Interleukin-5, mouse IL-5 also acts on B cells. It induces the proliferation of pre-activated B cells and their differentiation. High affinity and low affinity receptors for IL-5 are expressed in all hematopoietic and lymphoid cells.The low affinity receptor, CD125, has a molecular mass of 50 kDa (p60). The introduction of p60 into these cells generates a high affinity IL-5 receptor. The second subunit of the IL-5 receptor is identical with the larger subunit of the receptor for the colony stimulating factor GM-CSF (CD131). This subunit is involved also in the generation of a high affinity receptor for IL-3 and is being referred to as common beta.
Gene Symbol IL5
Gene ID 16191
Accession No. P04401
Source Insect cells
Appearance Lyophilized Powder
Molecular Weight 13.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Bioactivity The ED(50) was determined by the dose-dependent proliferation of TF-1 cells was ≤ 0.2 ng/mL, corresponding to a specific activity of ≥ 6.0 x 10^6 units/mg.
Formulation Recombinant Interleukin-5 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.