| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | IL-T |
| Biological Activity | |
| Expression System | |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Shipping | |
| Species | |
| Storage | |
| Target |
Background
IL-15 is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: IL-T.
Species origin: 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.
Endotoxin:<0.01 EU per 1 μg of the protein by the LAL method.
Biological significance and function
Functionally, IL-15 mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as Immunology & Inflammation.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Source species: Human
- Molecular weight: The protein has a calculated MW of 13.7 kDa. The protein migrates as 13 kDa under reducing condition (SDS-PAGE analysis).
- Protein length: The Human IL-15 consists of 114 amino acids and has a predicted molecular mass of 12.7 kDa
- Expression region: Amino acid sequence derived from Human IL-15 (Asn49-Ser162)(P40933) was expressedwas expressed with 6×His tag at the N-terminus
- Purity: >95% as determined by SDS-PAGE.
- Biological 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.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: His tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: The protein was lyophilized from a 0.2 µm filtered solution containing 1X PBS, pH 8.0. If you have any concerns or special requirements, please confirm with us.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.
What is the purity of Human IL-15 protein, His tag (Animal-Free) (Human)?
What buffer is this protein supplied in?
How should Human IL-15 protein, His tag (Animal-Free) (Human) be stored?
What expression system was used to produce this protein?
What is the molecular weight of this protein?
Is this protein biologically active?
What are the shipping conditions?
Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.