Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Additional Information | Soon to be discontinued. |
Details of Functionality | Measured by its ability to induce myeloperoxidase release from cytochalasin B-treated human neutrophils. Schröder, J.M. et al. (1987) J. Immunol. 139:3474. The ED50 for this effect is 0.1‑0.3 µg/mL. Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR2. The ED50 for this effect is 0.15-0.75 ng/mL. |
Source | E. coli-derived human CXCL5/ENA-70 protein Arg45-Asn114 |
Accession # | |
N-terminal Sequence | Arg45 |
Protein/Peptide Type | Recombinant Proteins |
Gene | CXCL5 |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 7.7 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. |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
CXCL5, also known as epithelial cell-derived neutrophil-activating peptide (ENA-78), is an 8 kDa proinflammatory member of the CXC subfamily of chemokines. Its Glu-Leu-Arg (ELR) motif confers angiogenic properties and distinguishes it from ELR- CXC chemokines which are angiostatic (1 - 3). Human CXCL5 shares 57% amino acid (aa) sequence identity with mouse and rat CXCL5. Among other human ELR+ chemokines, it shares 77% aa sequence identity with CXCL6/GCP-2 and 35% - 51% with CXCL1/GRO alpha, CXCL2/GRO beta, CXCL3/GRO gamma, CXCL7/NAP-2, and CXCL8/IL-8. Inflammatory stimulation upregulates CXCL5 production in multiple hematopoietic cell types, fibroblasts, endothelial cells, and vascular smooth muscle cells. In vivo, CXCL5 is elevated at sites of inflammation and pulmonary fibrosis where it promotes neutrophil infiltration and activation as well as angiogenesis (3 - 6). Its upregulation contributes to increased vascularization, tumor growth, and metastasis in many cancers (6 - 9). Full length CXCL5 (78 aa) is trimmed at the N‑terminal end by cathepsin G and chymotrypsin to ENA-74 (74 aa) and ENA-70 (70 aa), with the shortened forms showing increased potency relative to full length CXCL5 (10, 11). CXCL5 exerts its effects primarily through interactions with CXCR2 (6, 12). It also binds DARC, a decoy chemokine receptor which can limit CXCR2-mediated responses (13, 14).
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