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Recombinant Human IL-8/CXCL8 (Mucin Stalk Chimera), CF

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-8/CXCL8 (Mucin Stalk Chimera), CF Summary

Details of Functionality
Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR2. The ED50 for this effect is 5‑25 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human IL-8/CXCL8 protein
Human IL-8
(Ala23-Ser99) (Asn98Gly) &
(Ser28-Ser99) (Asn98Gly)
Accession # P10145		 Human Fractalkine Mucin-like Stalk
(Phe103-Gln341)
Accession # P78423 		KQN 6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala23 & Ser28
Protein/Peptide Type
Recombinant Proteins
Gene
CXCL8
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
34.8 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
80-95 kDa, reducing conditions
Publications
Read Publication using
968-IL/CF in the following applications:

Packaging, Storage & Formulations

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 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-8/CXCL8 (Mucin Stalk Chimera), CF

  • 3-10C
  • AMCF-I
  • C-X-C motif chemokine 8
  • CXCL8
  • CXCL8SCYB8
  • Emoctakin
  • GCP1
  • GCP-1TSG-1
  • IL8
  • IL-8
  • interleukin 8
  • K60
  • LAI
  • LECT
  • LUCT
  • LYNAP
  • MDNCF
  • MDNCFb-ENAP
  • member 8
  • MONAP
  • MONAPGCP1
  • NAF
  • NAP1
  • NAP-1NAP1
  • NCF
  • Neutrophil-activating protein 1
  • Protein 3-10C
  • T cell chemotactic factor
  • T-cell chemotactic factor
  • TCF
  • TSG1

Background

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). 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 CXCL8 shares 65%-69% amino acid (aa) sequence identiity with canine, feline, and porcine CXCL8 (4). There is no CXCL8 gene counterpart in rodent. N-terminal truncation by multiple proteases generates a range of shorter forms, and an alternative splice form of human CXCL8 carries an eleven aa substitution at the C-terminus (5). The bioactivity of CXCL8 is regulated by these truncations, by CXCL8 citrullination at Arg5 (N-terminal to the ELR motif) (6), and by the decoy receptor DARC (7). 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 CXCL8 interaction with CXCR1 (11). 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). In the CXCL8/IL-8 Mucin-like Stalk Chimera, the chemokine domain of human CX3CL1/Fractalkine is replaced by human CXCL8.
  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.

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Publications for CXCL8/IL-8 (968-IL/CF)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Binding Assay.


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Bioinformatics

Gene Symbol CXCL8
Uniprot