| 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.
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| Source: |
Escherichia Coli. |
| Physical Appearance: |
Sterile Filtered White lyophilized (freeze-dried) powder.
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| Formulation: |
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
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| 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.
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| 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.
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| 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.
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| 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.
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| 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.
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| Endotoxin: |
Less than 0.1 ng/µg (IEU/µg) of NAP-2.
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| 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.
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