MIP 4 Recombinant eiwit

Source : Escherichia Coli. Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques. Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine) . MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.

Small inducible cytokine A18||CCL18||Macrophage inflammatory protein 4||MIP-4||Pulmonary and activation-regulated chemokine||CC chemokine PARC||Alternative macrophage activation-associated CC chemokine 1||AMAC-1||Dendritic cell chemokine 1||DC-CK1||c

Greater than 97.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

MIP-4 protein is lyophilized from a 0.2μm filtered concentrated (1.0mg/mL) solution in 20mM PB, pH 7.4, 100mM NaCl.

Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) .Please prevent freeze-thaw cycles.

It is recommended to reconstitute the lyophilized MIP-4 in sterile 18M-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions. The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.