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Recombinant Human IL-6 Protein

Cat # Size Price Quantity
63170120 μg$200
631702100 μg$610

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
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)
SpeciesHuman
accession numberNP_000591.1
SourcesA DNA sequence encoding the mature form of human IL6 (NP_000591.1) (Val30-Met212) was expressed with an initial Met at the N-terminus.
Molecular WeightThe recombinant human IL6 consists of 184 amino acids and predicts a molecular mass of 20.95 kDa. It migrates as an approximately 19.7 kDa band in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity≥ 95 % as determined by SDS-PAGE
Regulatory StatusRUO
Endotoxin level<0.01EU 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.
Research AreasCytokines, Inflammation, Metabolism, Th17 cells, B cell Maturation, Megakaryocytes, Fever, Neurons, Autoimmunity

Background Information

Human interleukin-6 (IL-6) is a multifunctional cytokine produced by a wide range of cells, including macrophages, T cells, fibroblasts, and endothelial cells in response to infection or tissue injury. It plays a central role in immune regulation, inflammation, and hematopoiesis. IL-6 promotes differentiation of B cells into antibody-secreting plasma cells, supports T cell proliferation, and drives the acute phase response in the liver, leading to production of proteins such as C-reactive protein. It also influences metabolic and regenerative processes.

Structurally, IL-6 is a ~26 kDa glycoprotein composed of a four α-helix bundle typical of the cytokine family. IL-6 exerts its biological activity by binding to the IL-6 receptor (IL-6Rα), which exists in both membrane-bound and soluble forms. The IL-6/IL-6R complex then associates with the signal-transducing co-receptor gp130, triggering intracellular signaling cascades such as the JAK/STAT3, MAPK, and PI3K pathways. This dual signaling mechanism—classic signaling via membrane IL-6R and trans-signaling via soluble IL-6R—expands the range of IL-6-responsive cells.

Dysregulated IL-6 production is implicated in numerous diseases, including chronic inflammatory disorders (e.g., rheumatoid arthritis), autoimmune diseases, cytokine release syndrome, and cancer, where it can promote tumor growth and survival. Elevated IL-6 levels are also associated with severe infections and systemic inflammation. Therapeutically, targeting the IL-6 pathway has proven highly effective; monoclonal antibodies against IL-6 or IL-6R are widely used to treat inflammatory diseases and are also employed to manage cytokine storm syndromes. Conversely, IL-6 has been explored as a biomarker and, in some contexts, as a target to modulate immune and regenerative responses.

Data Sheets

Recombinant Human 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.