Recombinant Human Neutrophil Activating Protein-2 (CXCL7) - rHuNAP-2



Data Sheet
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Recombinant Human Neutrophil Activating Protein-2 (CXCL7) - rHuNAP-2

Description: Recombinant Human NAP-2 produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The rHuNAP-2 is purified by proprietary chromatographic techniques.
Source: Escherichia Coli.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Solubility: It is recommended to reconstitute the lyophilized rHuNAP-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability: Lyophilized rHuNAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18 C. Upon reconstitution rHuNAP-2 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 98.0% 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 Ala-Glu-Leu-Arg-Cys
Dimers and aggregates: Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
Biological Activity: ProSpec's NAP-2 is fully biologically active when compared to standard. The specific activity as determined by the ability of NAP-2 to chemoattract human neurotrophils using a concentration of 1-10 ng/ml.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of NAP-2.
Protein content: Protein quantitation was carried out by two independent methods: UV spectroscopy at 280 nm. Analysis by RP-HPLC, using a standard solution of NAP-2 as a Reference Standard.
Usage: This material is offered for research, laboratory or further manufacturing purposes.