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Recombinant Human IL-8/CXCL8 Protein

R&D Systems | Catalog # 208-IL

R&D Systems
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Key Product Details

  • R&D Systems E. coli-derived Recombinant Human IL-8/CXCL8 Protein (208-IL)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

Applications

Bioactivity
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Product Specifications

Source

E. coli-derived human IL-8/CXCL8 protein
Ser28-Ser99

Purity

>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ser28

Predicted Molecular Mass

8 kDa

Activity

Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR2.
The ED50 for this effect is 0.5-2.5 ng/mL.

Reviewed Applications

Read 8 reviews rated 4.9 using 208-IL in the following applications:

Scientific Data Images for Recombinant Human IL-8/CXCL8 Protein

Recombinant Human IL-8/CXCL8 Protein Bioactivity

Recombinant Human IL-8/CXCL8 Protein Bioactivity

Recombinant Human IL-8/CXCL8 (Catalog # 208-IL) chemoattracts the BaF3 mouse pro-B cell line transfected with human CXCR2. The ED50 for this effect is 0.5-2.5 ng/mL.
Recombinant Human IL-8/CXCL8 Protein SDS-PAGE

Recombinant Human IL-8/CXCL8 Protein SDS-PAGE

1 μg/lane of Recombinant Human IL-8/CXCL8 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 8 kDa.

Formulation, Preparation, and Storage

Carrier Free
What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Carrier: 208-IL
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Carrier Free: 208-IL/CF
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: IL-8/CXCL8

Interleukin-8 (IL-8), also known as CXCL8, GCP-1, and NAP-1, is a widely expressed proinflammatory member of the CXC family of chemokines. Near its N-terminus, this 8-9 kDa chemokine contains an ELR motif which is important for its angiogenic properties (1). IL-8/CXCL8 can associate into a homodimer or a heterodimer with CXCL4/PF4 (2), and it can also interact with matrix and cell surface glycosaminoglycans (3). Mature human IL-8/CXCL8 shares 65%-69% amino acid (aa) sequence identiity with canine, feline, and porcine IL-8/CXCL8 (4). There is no IL-8/CXCL8 gene counterpart in rodent. N-terminal truncation by multiple proteases generates a range of shorter forms, and an alternative splice form of human IL-8/CXCL8 carries an eleven aa substitution at the C-terminus (5). The bioactivity of IL-8/CXCL8 is regulated by these truncations, by IL-8/CXCL8 citrullination at Arg5 (N-terminal to the ELR motif) (6), and by the decoy receptor DARC (7). IL-8/CXCL8 effects are mediated through CXCR1/IL-8 RA, which is also used by CXCL6, and through CXCR2/IL-8 RB, which is used by multiple CXC chemokines (1). CXCR1 and CXCR2 associate into functional homodimers and heterodimers with each other (8). Through both CXCR1 and CXCR2, CXCL8 promotes neutrophil adhesion to the vascular endothelium and migration to sites of inflammation (9). It triggers the antimicrobial activation of neutrophils through CXCR1 (10). CXCL8 also binds to Serpin A1/alpha-1 Antitrypsin, and this prevents IL-8/CXCL8 interaction with CXCR1 (11). IL-8/CXCL8 is upregulated in atherosclerotic lesions and other cardiac pathologies where it exacerbates inflammatory tissue damage (12). In addition, it induces VEGF expression, vascular endothelial cell proliferation, angiogenesis, and tumor cell invasiveness (13-16).

References

  1. Lazennec, G. and A. Richmond (2010) Trends Mol. Med. 16:133.
  2. Nesmelova, I.V. et al. (2005) J. Biol. Chem. 280:4948.
  3. Pichert, A. et al. (2012) Biomatter 2:142.
  4. Schmid, J. and C. Weissmann (1987) J. Immunol. 139:250.
  5. Mortier, A. et al. (2008) Pharmacol. Ther. 120:197.
  6. Proost, P. et al. (2008) J. Exp. Med. 205:2085.
  7. Neote, K. et al. (1994) Blood 84:44.
  8. Munoz, L.M. et al. (2009) J. Immunol. 183:7337.
  9. Gerszten, R.E. et al. (1999) Nature 398:718.
  10. Jones, S.A. et al. (1996) Proc. Natl. Acad. Sci. USA 93:6682.
  11. Bergin, D.A. et al. (2010) J. Clin. Invest. 120:4236.
  12. Apostolakis, S. et al. (2009) Cardiovasc. Res. 84:353.
  13. Martin, D. et al. (2009) J. Biol. Chem. 284:6038.
  14. Li, A. et al. (2005) Angiogenesis 8:63.
  15. Waugh, D.J. and C. Wilson (2008) Clin. Cancer Res. 14:6735.
  16. Fernando, R.I. et al. (2011) Cancer Res. 71:5296.

Long Name

Interleukin 8

Alternate Names

CXCL8, GCP1, IL8, LAI, LECT, LUCT, LYNAP, MDNCF, MONAP, NAF, NAP1, NCF, TCF, TSG1

Entrez Gene IDs

3576 (Human); 396880 (Porcine); 403850 (Canine); 493836 (Feline)

Gene Symbol

CXCL8

UniProt

Additional IL-8/CXCL8 Products

Product Documents for Recombinant Human IL-8/CXCL8 Protein

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot or batch number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human IL-8/CXCL8 Protein

For research use only

Citations for Recombinant Human IL-8/CXCL8 Protein

Customer Reviews for Recombinant Human IL-8/CXCL8 Protein (8)

4.9 out of 5
8 Customer Ratings
5 Stars
88%
4 Stars
13%
3 Stars
0%
2 Stars
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1 Stars
0%

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Showing  1 - 5 of 8 reviews Showing All
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  • CXCL8 - Migration assay
    Name: Anonymous
    Application: Cell migration/motility
    Species: Human
    Verified Customer | Posted 04/24/2025
    Comparison of NK cell count/µL in the control condition (R10) vs CXCL8 at 10ng/mL
    200.000 sorted NK cells were place in the upper chamber of a 24 well plate with transwell inserts (5µm pore size). 650µL of culture media containing 10ng/mL of CXCL8 were placed in the lower chamber. Cell count was performed by flow cytometry using counting bead after one hour of migration at 37ºC.
    Recombinant Human IL-8/CXCL8 Protein 208-IL
  • Name: Anonymous
    Application: Cell Proliferation
    Verified Customer | Posted 08/14/2023
    Recombinant Human IL-8/CXCL8 Protein 208-IL
  • Recombinant Human IL-8/CXCL8 Protein
    Name: Anonymous
    Application: Cell migration/motility
    Verified Customer | Posted 03/15/2021
    The primary cells were starved overnight and treated with IL-8 (40ng/ml) and tested its effects on cell migration.
    Recombinant Human IL-8/CXCL8 Protein 208-IL
  • Recombinant Human IL-8/CXCL8 Protein
    Name: Anonymous
    Application: Assay validation
    Verified Customer | Posted 02/09/2021
  • Recombinant Human IL-8/CXCL8 Protein
    Name: Anonymous
    Application: In vitro bioactivity in cell culture
    Verified Customer | Posted 12/03/2018
    rhIL-8 induce beta -arrestin release in CXCR1/U2OS reporter cell line
    Recombinant Human IL-8/CXCL8 Protein 208-IL
  • Recombinant Human IL-8/CXCL8 Protein
    Name: Zoia Levashova
    Application: Immunoassay Standard
    Verified Customer | Posted 11/26/2018
    The recombinant human IL-8 protein was used as the calibration reagent in MSD assay with biotinylated MAB208 (capture) and Sulfo-Tag labeled AF-208-NA (detection) antibodies.
    Recombinant Human IL-8/CXCL8 Protein 208-IL
  • Recombinant Human IL-8/CXCL8 Protein
    Name: Anonymous
    Application: activation of neutrophils from blood in vitro.
    Verified Customer | Posted 11/10/2017
  • Recombinant Human IL-8/CXCL8 Protein
    Name: Michelle Chen
    Application: activation of neutrophils
    Verified Customer | Posted 04/07/2017
    Neutrophils were activated with 208-IL and assessed for morphological changes and migratory activity on 2D cell culture plate.
    Recombinant Human IL-8/CXCL8 Protein 208-IL

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FAQs for Recombinant Human IL-8/CXCL8 Protein

Showing  1 - 3 of 3 FAQs Showing All
  • Q: Are mouse or rat CXCL8/IL-8 products offered?

    A: Mouse and rat do not have a gene which encodes CXCL8/IL-8. In mouse, the functional homologs to human CXCL8/IL-8 are CXCL1/KC and CXCL2/MIP-2. In rat, the functional homolog to CXCL8/human IL-8 is CXCL3/CINC-2.

  • Q: Can Recombinant Human IL-8/CXCL8 Protein (Catalog # 208-IL) be used with mouse cells?

    A: Bioactivity of Recombinant Human IL-8/CXCL8 Protein (Catalog # 208-IL) has only been evaluated using human cells transfected with human CXCR2 (the human receptor for IL-8), and we have not evaluated the activity of this protein using mouse cells. There is no IL-8/CXCL8 gene counterpart in rodent species. We are aware of a few publications citing use of 208-IL in mouse assay systems, so we would recommend reviewing the publications listed on the Citations tab of the product-specific web page to find reported use of our products in similar experimental layouts.

  • Q: What is the difference between 208-IL (rhCXCL8/IL-8) and  618-IL (rhEndothelial Cell-Derived IL-8/CXCL8)?

    A: Several N-terminal processed forms of CXCL8/IL-8 are produced by proteolytic cleavage after secretion by cells such as peripheral blood monocytes, leukcocytes and endothelial cells. Catalog # 208-IL consists only of the sequence Ser28 to Ser99 (also known as IL-8, 6-77), which is the most prominent form of IL-8. According to literature, IL-8(6-77) has a 5-10-fold higher activity in neutrophil activation. Catalog # 618-IL consists of Ser28 to Ser99 (IL-8, 6-77) and Ala23 to Ser99 (IL-8).  In our chemoattraction assay, 208-IL has a 2-fold higher activity than 618-IL.Several N-terminal processed forms of CXCL8/IL-8 are produced by proteolytic cleavage after secretion by cells such as peripheral blood monocytes, leukcocytes and endothelial cells. Catalog # 208-IL consists only of the sequence Ser28 to Ser99 (also known as IL-8, 6-77), which is the most prominent form of IL-8. According to literature, IL-8(6-77) has a 5-10-fold higher activity in neutrophil activation. Catalog # 618-IL consists of Ser28 to Ser99 (IL-8, 6-77) and Ala23 to Ser99 (IL-8).  In our chemoattraction assay, 208-IL has a 2-fold higher activity than 618-IL.

  • Q: Are mouse or rat CXCL8/IL-8 products offered?

    A: Mouse and rat do not have a gene which encodes CXCL8/IL-8. In mouse, the functional homologs to human CXCL8/IL-8 are CXCL1/KC and CXCL2/MIP-2. In rat, the functional homolog to CXCL8/human IL-8 is CXCL3/CINC-2.

  • Q: Can Recombinant Human IL-8/CXCL8 Protein (Catalog # 208-IL) be used with mouse cells?

    A: Bioactivity of Recombinant Human IL-8/CXCL8 Protein (Catalog # 208-IL) has only been evaluated using human cells transfected with human CXCR2 (the human receptor for IL-8), and we have not evaluated the activity of this protein using mouse cells. There is no IL-8/CXCL8 gene counterpart in rodent species. We are aware of a few publications citing use of 208-IL in mouse assay systems, so we would recommend reviewing the publications listed on the Citations tab of the product-specific web page to find reported use of our products in similar experimental layouts.

  • Q: What is the difference between 208-IL (rhCXCL8/IL-8) and  618-IL (rhEndothelial Cell-Derived IL-8/CXCL8)?

    A: Several N-terminal processed forms of CXCL8/IL-8 are produced by proteolytic cleavage after secretion by cells such as peripheral blood monocytes, leukcocytes and endothelial cells. Catalog # 208-IL consists only of the sequence Ser28 to Ser99 (also known as IL-8, 6-77), which is the most prominent form of IL-8. According to literature, IL-8(6-77) has a 5-10-fold higher activity in neutrophil activation. Catalog # 618-IL consists of Ser28 to Ser99 (IL-8, 6-77) and Ala23 to Ser99 (IL-8).  In our chemoattraction assay, 208-IL has a 2-fold higher activity than 618-IL.Several N-terminal processed forms of CXCL8/IL-8 are produced by proteolytic cleavage after secretion by cells such as peripheral blood monocytes, leukcocytes and endothelial cells. Catalog # 208-IL consists only of the sequence Ser28 to Ser99 (also known as IL-8, 6-77), which is the most prominent form of IL-8. According to literature, IL-8(6-77) has a 5-10-fold higher activity in neutrophil activation. Catalog # 618-IL consists of Ser28 to Ser99 (IL-8, 6-77) and Ala23 to Ser99 (IL-8).  In our chemoattraction assay, 208-IL has a 2-fold higher activity than 618-IL.

  • Q: Are mouse or rat CXCL8/IL-8 products offered?

    A: Mouse and rat do not have a gene which encodes CXCL8/IL-8. In mouse, the functional homologs to human CXCL8/IL-8 are CXCL1/KC and CXCL2/MIP-2. In rat, the functional homolog to CXCL8/human IL-8 is CXCL3/CINC-2.

  • Q: Can Recombinant Human IL-8/CXCL8 Protein (Catalog # 208-IL) be used with mouse cells?

    A: Bioactivity of Recombinant Human IL-8/CXCL8 Protein (Catalog # 208-IL) has only been evaluated using human cells transfected with human CXCR2 (the human receptor for IL-8), and we have not evaluated the activity of this protein using mouse cells. There is no IL-8/CXCL8 gene counterpart in rodent species. We are aware of a few publications citing use of 208-IL in mouse assay systems, so we would recommend reviewing the publications listed on the Citations tab of the product-specific web page to find reported use of our products in similar experimental layouts.

  • Q: What is the difference between 208-IL (rhCXCL8/IL-8) and  618-IL (rhEndothelial Cell-Derived IL-8/CXCL8)?

    A: Several N-terminal processed forms of CXCL8/IL-8 are produced by proteolytic cleavage after secretion by cells such as peripheral blood monocytes, leukcocytes and endothelial cells. Catalog # 208-IL consists only of the sequence Ser28 to Ser99 (also known as IL-8, 6-77), which is the most prominent form of IL-8. According to literature, IL-8(6-77) has a 5-10-fold higher activity in neutrophil activation. Catalog # 618-IL consists of Ser28 to Ser99 (IL-8, 6-77) and Ala23 to Ser99 (IL-8).  In our chemoattraction assay, 208-IL has a 2-fold higher activity than 618-IL.Several N-terminal processed forms of CXCL8/IL-8 are produced by proteolytic cleavage after secretion by cells such as peripheral blood monocytes, leukcocytes and endothelial cells. Catalog # 208-IL consists only of the sequence Ser28 to Ser99 (also known as IL-8, 6-77), which is the most prominent form of IL-8. According to literature, IL-8(6-77) has a 5-10-fold higher activity in neutrophil activation. Catalog # 618-IL consists of Ser28 to Ser99 (IL-8, 6-77) and Ala23 to Ser99 (IL-8).  In our chemoattraction assay, 208-IL has a 2-fold higher activity than 618-IL.

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