Recombinant Human IL-7 Protein

Cat # Size Price Quantity
63390110 μg$160
633902100 μg$750

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH7.4.
Expression HostE.coli
Target NameIL-7, Interleukin 7, Lymphopoietin-1 (LP-1)
SpeciesHuman
accession numberNP_000871.1
SourcesA DNA sequence encoding the mature form of human IL7 (NP_000871.1)(Asp26-His177) was expressed with a N-terminal Met.
Molecular WeightThe recombinant human IL7 consists of 153 amino acids and predicts a molecular mass of 17.5 KDa. It migrates as an approximately 20.4 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< 0.1 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples 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.

Background Information


Human interleukin-7 (IL-7) is a cytokine essential for lymphocyte development, survival, proliferation, and immune homeostasis. It is produced primarily by stromal cells in the bone marrow and thymus, as well as by epithelial and other non-hematopoietic cells in lymphoid tissues. IL-7 is particularly important for the development of T lymphocytes and the maintenance of naïve and memory T cells. It also supports early B-cell development in humans and helps preserve a diverse, functional adaptive immune system.



Human IL-7 is a secreted glycoprotein consisting of 177 amino acids in its precursor form, including a signal peptide that is removed during secretion. The mature cytokine contains approximately 152 amino acids and adopts a characteristic four-helix bundle structure shared by class I hematopoietic cytokines. IL-7 functions as a soluble ligand that binds to a specific cell-surface receptor complex composed of the IL-7 receptor alpha chain (IL-7Rα/CD127) and the common gamma chain (γc/CD132), which is shared by several other cytokine receptors.



IL-7 binding induces receptor-associated signaling, primarily through JAK1 and JAK3, leading to activation of STAT5 and additional pathways, including PI3K/AKT. These signals promote lymphocyte survival by regulating anti-apoptotic proteins, support cell proliferation, and influence T-cell differentiation and homeostasis. IL-7 signaling is tightly regulated to maintain immune balance.



Abnormal IL-7 or IL-7 receptor signaling is associated with several diseases. Impaired signaling can cause severe immune deficiency, whereas excessive activity may contribute to autoimmune disorders, including multiple sclerosis and inflammatory conditions. Dysregulated IL-7 receptor signaling is also implicated in certain hematologic malignancies, particularly T-cell acute lymphoblastic leukemia, where activating mutations in IL7R can promote uncontrolled cell growth. Therapeutically, recombinant IL-7 has been investigated to restore or expand T-cell populations in patients with lymphopenia, cancer, or chronic infections. Conversely, blocking IL-7 or IL-7R signaling is being explored for autoimmune and inflammatory diseases, while IL-7-based approaches may enhance immune-cell expansion in cancer immunotherapy.

Data Sheets


Recombinant Human IL-7 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.

Have a product or application question? Consult our FAQs or contact us.