Source:

Escherichia coli.

Molecular Weight:

8.4 kDa, observed by reducing SDS-PAGE.

Purity:

> 95% as analyzed by SDS-PAGE and HPLC.

Biological activity:

ED50 < 20 ng/mL, measured by the FLIPR assay using CHO cells transfected with human CXCR1, the receptor of human CXCL8, corresponding to a specific activity of > 5×10ˆ4 units/mg.

AA Sequence:

SAKELRCQ CIKTYSKPFH PKFIKELRVI ESGPHCANTE IIVKLSDGRE LCLDPKENWV QRVVEKFLKR AENS

Endotoxin:

< 0.2 EU/μg, determined by LAL method.

Formulation:

Lyophilized after extensive dialysis against PBS.

Background:

Interleukin-8 is one of the first discovered chemokines, and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. In vivo, IL-8 exists in two forms: 77 a.a. produced by endothelial cells, and the more active 72 a.a. produced by monocytes. The receptors of IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cellular shape, activate the integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells.Recombinant human I Interleukin-8/CXCL8 (rhIL-8) produced in E.coli is a single non-glycosylated polypeptide chain containing 72 amino acids. A fully biologically active molecule, rhIL-8 has a molecular mass of 8.4 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.

Usage:

This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Reconstitution:

Reconstituted in ddH2O at 100 μg/mL.

Storage:

Lyophilized recombinant human Interleukin-8/CXCL8 (rhIL-8) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhIL-8 remains stable up to 2 weeks at 4°C or up to 3 months at -20°C.