Reactivity | RtSpecies Glossary |
Applications | Bioactivity |
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 3-6 µg/mL. Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR2. The ED50 for this effect is 4-20 ng/mL. |
Source | E. coli-derived rat CXCL3/GRO gamma/CINC-2/DCIP-1 protein Arg33-Ser100 |
Accession # | |
N-terminal Sequence | Arg33 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Cxcl3 |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 7.6 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. |
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 with BSA as a carrier protein. |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 50 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
The rat chemokines CINC (cytokine-induced neutrophil chemoattractant)-1, CINC-2 alpha , CINC-2 beta and CINC-3 (also named MIP-2) constitute a group of rat CXC chemokines that show significant sequence similarity to human GROs and mouse MIP-2 but not IL-8. CINC-2 alpha , CINC-2 beta were originally purified as novel neutrophil chemoattractants from the conditioned medium of rat granulation tissue which also contain CINC-1 and CINC-3. Based on amino acid (aa) sequence analysis of the purified CINC-2 alpha protein and sequencing of the CINC-2 beta cDNA clone, both mature CINC-2 alpha and CINC-2 beta were shown to contain 68 aa residues. The amino acid sequences of the two CINC-2 proteins are identical except for three carboxy-terminal residues. CINC-2 beta cDNA encodes a 100 aa residue precursor protein with a 32 aa residue signal peptide that is removed to yield the mature secreted protein. At the protein sequence level, mature CINC-2 proteins are 63% identical to CINC-1 and 80% identical to CINC-3. CINC-2 proteins represent the major chemokines purified from conditioned medium of granulation tissue or LPS-induced inflammatory exudate. Other cell types known to produce CINC-2 proteins include activated macrophages and fibroblasts.
Recombinant and natural CINC-2 proteins have been shown to be specific neutrophil chemoattractants both in vivo and in vitro. On the basis of cross-desensitization results of the various CINC proteins, it has been postulated that rat neutrophils have at least two classes of CINC receptors: a class of CINC-3-specific receptor as well as a second common receptor shared by all CINCs.
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