Human recombinant IL-15 (Interleukin-15) protein, AF

IL15 protein, Human

Interleukin-15 (IL-15) is a 14-15 kDa glycoprotein with immune regulatory functions in many diverse cell types. IL-15 can be constitutively expressed in a variety of cell types stored as intracellular protein in the cytoplasm as well as transport to the cell surface, while only secreted from some cell types including monocytes, dendritic cells, epithelial cells, bone marrow stromal cells, and fibroblasts. As a pleiotropic cytokine, IL-15 mediates the crosstalk between innate immunity and adaptive immunity whose principal role is to kill virally infected cells. IL-15 plays a crucial role in the development, differentiation, and survival of NK cells. In monocytes, IL-15 induces the production of IL-8 and monocyte chemotactic protein 1 (MCP-1), which recruits neutrophils and monocytes to sites of infection. IL-15 can also act as a chemo-attractant in T lymphocytes and regulate the differentiation of T lymphocytes.

Product Info Summary

SKU: PROTP40933-5
Size: 5ug,20ug,100ug
Origin Species: Human
Source: Escherichia coli
Application: Cell Culture

Product Name

Human recombinant IL-15 (Interleukin-15) protein, AF

View all IL15 recombinant proteins

SKU/Catalog Number

PROTP40933-5

Size

5ug,20ug,100ug

Tag

His Tag (N-term)

Description

Interleukin-15 (IL-15) is a 14-15 kDa glycoprotein with immune regulatory functions in many diverse cell types. IL-15 can be constitutively expressed in a variety of cell types stored as intracellular protein in the cytoplasm as well as transport to the cell surface, while only secreted from some cell types including monocytes, dendritic cells, epithelial cells, bone marrow stromal cells, and fibroblasts. As a pleiotropic cytokine, IL-15 mediates the crosstalk between innate immunity and adaptive immunity whose principal role is to kill virally infected cells. IL-15 plays a crucial role in the development, differentiation, and survival of NK cells. In monocytes, IL-15 induces the production of IL-8 and monocyte chemotactic protein 1 (MCP-1), which recruits neutrophils and monocytes to sites of infection. IL-15 can also act as a chemo-attractant in T lymphocytes and regulate the differentiation of T lymphocytes.

Storage & Handling

Lyophilized protein should be stored at -20°C for 1 year. Upon reconstitution, store at 2°C to 8°C for up to 1 week. Further dilute in a buffer containing a carrier protein or stabilizer (e.g. 0.1% BSA, 10%FBS, 5%HSA or 5% trehalose solution), protein aliquots should be stored at -20°C or -80°C for 3-6 months. Avoid repeated freeze/thaw cycles.

Cite This Product

Human recombinant IL-15 (Interleukin-15) protein, AF (Boster Biological Technology, Pleasanton CA, USA, Catalog # PROTP40933-5)

Form

Lyophilized

Formulation

The protein was lyophilized from a 0.2 μm filtered solution of NaPi buffer, 0.018% SDS, pH 7.5.containing 1X PBS, pH 8.0. If you have any concerns or special requirements, please confirm with us.

Purity

>95% as determined by SDS-PAGE.

Predicted MW

18.1 kDa

Molecular weight

The protein has a calculated MW of 13.7 kDa. The protein migrates as 13 kDa under reducing condition (SDS-PAGE analysis).

Activity

Measure by its ability to induce proliferation in CTLL-2 cells. The ED50 for this effect is <3 ng/mL. The specific activity of recombinant human IL-15 is > 2 x 106 IU/mg.

Endotoxin

<0.01 EU per 1 μg of the protein by the LAL method.

Amino Acid Sequence

NWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIHDTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFIN TS with polyhistidine tag at the N-terminus.

Reconstitution

Centrifuge at 3000 rpm for 5 mins before opening. It is recommended to reconstitute the lyophilized protein in sterile H2O to a concentration not less than 100 μg/mL and incubate the stock solution at room temperature for at least 20 mins to ensure sufficient re-dissolved. Do Not Vortex! Vigorous shaking may impair the biological activity of the protein.

Validation Images & Assay Conditions

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Size

Total: $77

SKU:PROTP40933-5

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Update date: Apr 2, 2026