Recombinant Human C-C Motif Chemokine 8/CCL8/MCP-2 (C-6His)

Recombinant Human C-C Motif Chemokine 8/CCL8/MCP-2 (C-6His)

Catalog Number:
P001411081ABE
Mfr. No.:
Abe32-7930
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      • Overview
        • MW : 9.95kD. Recombinant Human C-C Motif Chemokine 8 is produced by our Mammalian expression system and the target gene encoding Gln24-Pro99 is expressed with a 6His tag at the C-terminus. Human Chemokine (C-C Motif) Ligand 8 (CCL8) is produced by human MG63 osteosarcoma cells. CCL8 shares 62% and 58% amino acid sequence identity with MCP-1 and MCP-3, respectively. All three MCP proteins are monocyte chemoattractants. CCL8 is chemotactic for and activates many different immune cells, including mast cells, eosinophils and basophils, which are implicated in allergic response, and monocytes, T cells, and NK cells that are involved in the inflammatory response. CCL8 elicits its effects by binding to several different cell surface receptors including CCR1, CCR2B and CCR5.

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      • Properties
        • Source
          Human cells
          Type
          Recombinant Proteins
          Formulation
          Lyophilized from a 0.2 µm filtered solution of 20mM PB, 150mM NaCl, 1mM EDTA, pH 7.4.
          Storage
          Lyophilized protein should be stored at -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at -20°C for 3 months.
          Endotoxin
          Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

          More Information

          UniProt
          Gene ID
          6355

          * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

      • Applications
        • Application Description
          Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 µg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

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