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Recombinant Human IL15

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Product Source Size Cat. No. Price
Recombinant Human IL15 E. coli10 µg Z100455 $130.00
1.0 mg Z100459 $2,700.00
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Data Sheet
Print Version
Alternative Names IL-15, IL-T
Recombinant Human Interleukin-15 (IL15)
Description IL-15 has been shown to be produced by human fetal astrocytes and microglial cells in response to IL-1-beta, IFN-gamma, or TNF-alpha and may thus play a role in T cell mediated immune responses in the human central nervous system. IL-15 stimulates proliferation of the established T cell line CTLL-2, CD8(+) memory T cells require IL-15 for proliferation. IL-15 is also able to induce generation of cytolytic cells and LAK cells activity in vitro. IL-15 appears to function as a specific maturation factor for natural killer cells and can mimic the bone marrow microenvironment in vitro, which is required for natural killer cells to acquire lytic functions. IL-15 induces proliferation of mast cells in the absence of functional IL-2 receptor components and utilizes a receptor of 60-65 kDa that is distinct from known components of T cell IL-15 receptors. The IL-15 receptor on mast cells recruits JAK2 and STAT5, instead of JAK1, JAK3 and STAT3 and STAT5 that are activated in T cells. The alpha subunit of the IL-15 receptor (IL-15RA) is structurally related to the alpha subunit of the IL-2 receptor and confers high affinity binding of IL-15 to its receptor. IL-15 binds to the beta and gamma chains of the IL-2 receptor, which are known to be required for ligand internalization and signal transduction.
Gene Symbol IL15
Gene ID 3600
Accession No. P40933
Source E. coli
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
Gel Image Click To Enlarge
Bioactivity The ED(50) as determined by the dose-dependent proliferation of T lympocytes was <0.1ng/ml.
Bioactivity Data Click To Enlarge
Formulation Recombinant IL-15 was lyophilized from a 0.2 μm filtered PBS solution pH 7.5.
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.