Recombinant Human Macrophage Inflammatory protein-3 beta (CCL19) - rHuMIP-3b



Data Sheet
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Recombinant Human Macrophage Inflammatory protein-3 beta (CCL19) - rHuMIP-3b

Description: Recombinant Human MIP-3b produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8809 Dalton. rHuMIP-3b is purified by proprietary chromatographic techniques.
Source: Escherichia Coli.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Solubility: It is recommended to reconstitute the lyophilized MIP-3β in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability: Lyophilized MIP-3β although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-3b 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.
Purity: Greater than 99.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
Amino acid sequence: The sequence of the first five N-terminal amino acids was determined and was found to be, Gly-Thr-Asn-Asp-Ala.
Dimers and aggregates: Less than 1% as determined by silver-stained SDS-PAGE gel.
Biological Activity: ProSpec’s rHuMIP-3β is fully biologically active when compared to standard. The Activity is calculated by the ability to chemoattract Human T cells using a concentration of 10-50 ng/ml.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of rHuMIP-3β.
Protein content: Protein quantitation was carried out by two independent methods: UV spectroscopy at 280 nm. Analysis by RP-HPLC, using a calibrated solution of MIP-3β as a Reference Standard.
Usage: This material is offered for research, laboratory or further manufacturing purposes.