Reactivity | RtSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR2. The ED50 for this effect is 0.03-0.15 µg/mL. |
Source | E. coli-derived rat LIX protein Ala38-Arg125 & Ala38-Lys117 |
Accession # | |
N-terminal Sequence | Ala38 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Cxcl6 |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 10.1 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. |
LPS-induced CXC chemokine (LIX) is a chemokine originally cloned from LPS-stimulated mouse fibroblasts. Rat LIX shares approximately 74% amino acid (aa) sequence identity with mouse LIX and is likely the rat orthologue to mouse LIX. Rat LIX cDNA encodes a 130 aa residue precursor with a predicted 37 aa residue signal peptide and a 93 aa residue mature protein. Among human CXC chemokines, rat LIX is most closely related to human GCP-2 and ENA-78. Rat LIX also differs from these two human proteins by having an extended carboxy-terminus. The amino-terminal 115 residues of rat LIX shares 59% and 53% aa sequence homology with human GCP-2 and ENA-78, respectively. It is not clear if LIX should be considered an orthologue of GCP-2 or ENA-78. Yet, mouse LIX was alternatively named mouse GCP-2.
Purified recombinant rat LIX is C-terminally truncated. This is consistent with the observation that natural mouse LIX purified from fibroblasts and epithelial cells also contains multiple amino-terminal and carboxy-terminal truncated isoforms. The shorter isoforms of the natural protein were reported to be more active than the longer forms. The bioactivity of rat LIX can be mediated through CXCR2.
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