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| Full Name | |
| Abbreviated Name-1 | rHuIGF-2; rHuIGF2 |
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| Abbreviated Name-2 | Insulin-Like Growth Factor-2; Insulin-Like Growth Factor2 |
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| Description | IGF-II also known as multiplication stimulating activity (MSA), shows virtually identical bioactivities as IGF-I. Expression of IGF-II is highest in fetal tissues, where it is believed to play a major role in overall growth and development. After birth IGF-II expression decreases to much lower levels in a variety of tissues. IGF-II is produced also in several tumors. IGF-II binds to IGF-II receptor (IGF-IIR), to IGF-IR and weakly to the insulin receptor (IR). All IGF-II bioactivities in adult tissues are generally attributed to its interaction with IGF-IR. However, during embryogenesis the roles of both IGF-IIR and IR may be significant in promoting normal growth. Recombinant Human IGF-2 produced in E. coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids and having a molecular mass of 7,505 Da. GenScript Insulin-Like Growth Factor (IGF)-2, human is purified by proprietary chromatographic techniques. |
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| Source | E. coli |
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| M.W. | 7,505 Da |
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| Purity | Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE |
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| Endotoxin Level | Less than 0.1 ng/µg (IEU/µg) of rHuIGF-2 |
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| Specific Activity | The ED50, calculated by the competitive binding of IGF-II plasma derived to human placental membrane is < 1.0 ng/ml, corresponding to a specific activity of 106 U/mg. |
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| Storage | Lyophilized rHuIGF-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rHuIGF-II 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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| Formulation | The protein was lyophilized with no additives. |
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| Reconstitution | It is recommended to reconstitute the lyophilized rHuIGF-II in sterile 18 MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. |
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| Quantitation | Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm.
2. Analysis by RP-HPLC, using a calibrated solution of IGF-2 as a Reference Standard. |
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| Sequence analysis | The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Tyr-Arg-Pro-Ser.
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