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Recombinant Human IL-2 Protein

Cat # Size Price Quantity
63090120 µg$180
630902100 µg$400

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostHEK293
Target NameIL-2, T-cell growth factor (TCGF)
SpeciesHuman
accession numberNP_000577.2
SourcesA DNA sequence encoding the human IL2 (NP_000577.2) (Ala21-Thr153) was expressed.
Molecular WeightThe recombinant human IL2 consists of 133 amino acids and predicts a molecular mass of 15.4 kDa. It migrates as an approximately 18.52 KDa band in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity> 95 % as determined by SDS-PAGE. > 95 % as determined by SEC-HPLC.
Regulatory StatusRUO
Endotoxin level<0.01EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingProteins are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Research AreasCytokines, Inflammation, Autoimmunity, T cells, Tregs, NK cells, B cells, Cancer Immunology

Background Information

Human interleukin-2 (IL-2) is a central cytokine in adaptive immunity that regulates T cell proliferation, survival, and differentiation. It is primarily produced by activated CD4+ T cells following antigen recognition and serves as a key growth factor for both effector and regulatory T cells. IL-2 promotes clonal expansion of antigen-specific lymphocytes, enhances cytotoxic activity of CD8+ T cells and natural killer (NK) cells, and plays a crucial role in maintaining immune tolerance through the development and function of regulatory T cells (Tregs).

Structurally, IL-2 is a small, single-chain α-helical cytokine that signals through a heterotrimeric receptor complex composed of IL-2Rα (CD25), IL-2Rβ (CD122), and the common γ chain (γc, CD132), which is shared with several other cytokines. The affinity of IL-2 binding varies depending on receptor subunit composition, with the high-affinity receptor including all three chains. Ligand binding triggers activation of JAK1 and JAK3 kinases and downstream STAT5 signaling, along with PI3K/AKT and MAPK pathways, leading to cell proliferation and survival. IL-2 functions as the primary ligand for this receptor system.

Dysregulation of IL-2 signaling is associated with autoimmune diseases, immunodeficiency, and cancer. Reduced IL-2 activity can impair immune tolerance, while excessive signaling may contribute to inflammation. Therapeutically, recombinant IL-2 has been used to treat cancers such as melanoma and renal cell carcinoma. More recently, engineered IL-2 variants and low-dose IL-2 therapies are being developed to selectively expand Tregs for autoimmune disease treatment.

Data Sheets

Recombinant Human IL-2 Protein TDS

Frequently Asked Questions

What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.
What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.
How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.
Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.
Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

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