Recombinant Mouse IL-6 Protein

Cat # Size Price Quantity
67050120 μg$200
670502100 μg$550

Product Details


ApplicationBioassay
FormatLyophilized from sterile 50 mM HAc, pH3.0
Expression HostE.coli
Target NameIL-6, Interleukin-6, B cell stimulating factor-2 (BSF-2), Cytotoxic T cell differentiation factor (CDF), Hybridoma/plasmacytoma growth factor (HPGF), Hepatocyte stimulating factor (HSF)
SpeciesMouse
accession numberP08505
SourcesA DNA sequence encoding the mouse IL6 (P08505) (Phe25-Thr211) was expressed and purified.
Molecular WeightThe recombinant mouse IL6 consists of 188 amino acids and predicts a molecular mass of 21.9 KDa. It migrates as an approximately 22 KDa band in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity> 90 % as determined by SDS-PAGE.
Regulatory StatusRUO
Endotoxin level< 1.0 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


Mouse interleukin-6 (IL-6) is a multifunctional cytokine that regulates immune responses, inflammation, hematopoiesis, and tissue repair. It is produced by a variety of cells, including macrophages, monocytes, T cells, endothelial cells, and fibroblasts, particularly following infection, tissue injury, or inflammatory stimulation. IL-6 promotes B-cell differentiation into antibody-producing plasma cells, influences T-cell differentiation, and stimulates hepatocytes to produce acute-phase proteins that contribute to the systemic inflammatory response.



Mouse IL-6 is a secreted glycoprotein belonging to the IL-6 cytokine family. Its mature protein adopts a characteristic four-alpha-helix bundle structure, which supports interactions with its receptor complex. IL-6 signals through the IL-6 receptor alpha chain (IL-6R/CD126) and the signal-transducing glycoprotein 130 (gp130/CD130). IL-6 first binds IL-6R, which exists in membrane-bound and soluble forms; the resulting complex recruits gp130 and activates intracellular pathways, including JAK/STAT3, MAPK, and PI3K–AKT. Unlike some cytokines, IL-6 does not have multiple unrelated conventional ligands; IL-6R and gp130 are its principal receptor components.



Dysregulated IL-6 signaling contributes to chronic inflammation, autoimmune disorders, and cancer-associated inflammation. In mouse disease models, elevated IL-6 activity has been implicated in experimental arthritis, inflammatory bowel disease, systemic autoimmunity, and tumor progression. However, IL-6 also supports antimicrobial defense and tissue regeneration, so its biological effects depend on the signaling context and disease environment.



Therapeutically, IL-6 is an important target for controlling pathological inflammation. Antibodies that neutralize IL-6 or block IL-6R can reduce excessive cytokine signaling, while selective inhibition of IL-6 trans-signaling may suppress inflammatory activity while preserving some beneficial functions of classic signaling. Mouse IL-6 and IL-6 pathway inhibitors are widely used in preclinical studies investigating inflammation, immune regulation, and therapeutic efficacy.

Data Sheets


Recombinant Mouse IL-6 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.