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    Recombinant human IL-8 protein

    QK119

    Brand: Qkine

    Interleukin-8 (IL-8) is an inflammatory cytokine that acts as a chemoattractant to neutrophils. It promotes the differentiation of hematopoietic progenitors into monocytic lineages including megakaryocytes, monocytes and macrophages. IL-8 can be used for the culture and differentiation of reproducible and high-quality hematopoietic stem cells and proliferation and migration in relevant cells.

    Qkine recombinant human IL-8 has a molecular weight of 8.9 kDa. This protein is animal origin-free, carrier-free and tag-free to ensure its purity with exceptional lot-to-lot consistency.

    Currency: 

    Product name Catalog number Pack size Price Price (USD) Price (GBP) Price (EUR)
    Recombinant human IL-8 protein, 25 µg QK119-0025 25 µg (select above) $ 210.00 £ 115.00 € 175.00
    Recombinant human IL-8 protein, 50 µg QK119-0050 50 µg (select above) $ 315.00 £ 225.00 € 263.00
    Recombinant human IL-8 protein, 100 µg QK119-0100 100 µg (select above) $ 500.00 £ 375.00 € 438.00
    Recombinant human IL-8 protein, 500 µg QK119-0500 500 µg (select above) $ 1,995.00 £ 1,475.00 € 1,723.00
    Recombinant human IL-8 protein, 1000 µg QK119-1000 1000 µg (select above) $ 3,100.00 £ 2,300.00 € 2,687.00

    Note: prices shown do not include shipping and handling charges.

    Qkine company name and logo are the property of Qkine Ltd. UK.

    Alternative protein names
    Interleukin-8, C-X-C motif chemokine 8, Chemokine (C-X-C motif) ligand 8, Emoctakin, Granulocyte chemotactic protein 1 (GCP-1), Monocyte-derived neutrophil chemotactic factor (MDNCF), Monocyte-derived neutrophil-activating peptide (MONAP), Neutrophil-activating protein 1 (NAP-1), Protein 3-10C, T-cell chemotactic factor, IL 8, IL8
    Species reactivity
    • human
    • species similarity:
    • mouse - 80%
    • bovine - 76%
    • porcine -76%

    Frequently used together:

    Summary

    • High purity human protein (Uniprot: P10145)
    • 8.9 kDa (monomer)
    • >98%, by SDS-PAGE quantitative densitometry
    • Expressed in E. coli
    • Animal origin-free (AOF) and carrier protein-free
    • Manufactured in Qkine's Cambridge, UK laboratories
    • Lyophilized from acetonitrile, TFA
    • Resuspend in 10 mM HCl (Reconstitution solution A) at >50 µg/ml, add carrier protein if desired, prepare single-use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term)
    Handling and Storage FAQ

    Featured applications

    • Differentiation into monocytic lineages
    • Chemotaxis experiments
    • Differentiation of osteoclasts

    Bioactivity

    Recombinant IL-8 activity was determined using an IL-8-responsive firefly luciferase reporter assay. Transfected HEK293T cells were treated in triplicate with a serial dilution of IL-8 for 3 hours. Firefly activity was measured and normalized to the control Renilla luciferase activity. Data from Qk119 lot #204742. EC50 = 49 ng/ml (5.44 nM).

    Qk119-Datasheet-graph_-Website

    Purity

    Recombinant IL-8 migrates as a major band at approximately 11 kDa in reduced (R) and non-reduced (NR) conditions. No contaminating protein bands are present. The purified recombinant protein 3 µg was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk119 lot #204742.

    IL-8-gel-1024x1024

    Further quality assays

    • Mass spectrometry: single species with expected mass
    • Recovery from stock vial:  >95%
    • Endotoxin: <0.005 EU/μg protein (below level of detection)

    Protein background

    Interleukin-8 (IL-8 or CXCL8) is a C-X-C motif family chemokine. IL-8 was originally identified through its chemotactic activity on neutrophil and named monocyte-derived neutrophil chemotactic factor (MDNCF) [1]. IL-8 is translated as 99 amino acid precursor before processing to the 72 amino acid biologically active form. In humans IL-8 has 2 receptors, CXCR1 and CXCR2, both G-protein coupled receptors [1, 4]. Binding of IL-8 to its receptors activates downstream pathways including Akt/PKB, MAPK, and PKC, regulating cell adhesion and migration.

    IL-8 is an inflammatory cytokine produced by several cell types including fibroblasts, lung epithelial cells, endothelial cells, keratinocytes, T cells, neutrophils, mast cells, monocytes and macrophages [2, 4]. As well as its role in inflammation IL-8 has been shown to play a role in tumor growth and vascularization. In triple negative breast cancer, IL-8 expression is closely related to prognosis and is being investigated as a potential therapeutic target [3].

    IL-8 also acts as a growth factor for human hematopoietic progenitors, promoting the growth and differentiation of cells of monocytic lineages including megakaryocytes, monocytes and macrophages [4]. Recombinant IL-8 has been shown to stimulate differentiation of human peripheral blood mononuclear cells into osteoclasts [5].

    Background references

    1. Matsushima K, Yang D and Oppenheim JJ, Interleukin-8: An evolving chemokine, Cytokine (2022). doi.org/10.1016/j.cyto.2022.155828.
    2. Benakanakere M, Finoti L, Tanaka U et al. Investigation of the functional role of human Interleukin-8 gene haplotypes by CRISPR/Cas9 mediated genome editing. Sci Rep 6 (2016). doi.org/10.1038/srep31180
    3. Deng F, Weng Y, Li X et al. Overexpression of IL-8 promotes cell migration via PI3K-Akt signaling pathway and EMT in triple-negative breast cancer, Pathology - Research and Practice (2020). doi.org/10.1016/j.prp.2020.152902.
    4. Corre I, Pineau D and Hermouet S. Interleukin-8: an autocrine/paracrine growth factor for human hematopoietic progenitors acting in synergy with colony stimulating factor-1 to promote monocyte-macrophage growth and differentiation. Exp Hematol. (1999). doi: 10.1016/s0301-472x(98)00032-0.
    5. Bendre MS, Montague DC, Peery T et al. Interleukin-8 stimulation of osteoclastogenesis and bone resorption is a mechanism for the increased osteolysis of metastatic bone disease. Bone (2003). doi.org/10.1016/S8756-3282(03)00086-3.

    FAQ

    What is IL-8?
    IL-8 is a proinflammatory cytokine which attracts neutrophils to the site of inflammation.

    Where is IL-8 found?
    IL-8 is a soluble protein found in serum. IL-8 is secreted by mononuclear macrophages, neutrophils, eosinophils, T lymphocytes, epithelial cells, and fibroblasts. It is also secreted by tumor cells and promotes tumor migration, invasion, angiogenesis, and metastasis.

    Is IL-8 a cytokine?
    Yes IL-8 is a cytokine

    What does the IL-8 gene do?
    IL-8 is encoded by the CXCL8, IL-8 gene expression is induced by a wide variety of agents including cytokines, growth factors, bacterial and viral products and oxidants.

    What does IL-8 bind to?
    IL-8 has two receptors CXCR1 and CXCR2

    What is the function of the IL-8 receptor?
    Both IL-8 receptors are G protein coupled and cause an increase in cGMP and activate Akt/PKB, MAPK, and PKC, regulating cell adhesion and migration.

    What is the IL-8 pathway?
    IL-8 binding to CXCR1 and CXCR2 activates various downstream molecules, including G proteins, small GTPases (Ras, Rac, Rho), and kinases (PI3K, PLC, PKC, AKT). This activates cell adhesion, actin polymerization, membrane protrusion, and eventually cell migration.

    How is IL-8 used in cell culture?
    IL-8 can be used to differentiate pluripotent cells into monocytic lineages or osteoclasts. IL-8 can also be used in chemotaxis studies.