| Catalog No. |
Size |
Price |
Figures |
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Z00368-10 ug
| 10 ug | $ 39.00 |
STRUCTURE:
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References:
- Yu J, et al. Interleukin-2 reconstitutes defective human immunodeficiency virus (HIV), and cytomegalovirus (CMV) specific CD8+ T cell proliferation in HIV infection. J. Med. Virol. Sep 2006; 78 (9): 1147-1157.
- Perchonock CE, et al. Negative Regulation of Interleukin-2 and p38 Mitogen-Activated Protein Kinase during T-Cell Activation by the Adaptor ALX. Mol. Cell. Biol. Aug 2006; 26 (16): 6005-6015.
- Gujar SA, Michalak TI. Characterization of bioactive recombinant woodchuck interleukin-2 amplified by RLM-RACE and produced in eukaryotic expression system. Vet. Immunol. Immunopathol. Aug 2006; 112 (3-4): 183-198.
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Z00368-50 ug
| 50 ug | $ 130.00 |
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Z00368-1 mg
| 1 mg | $ 500.00 |
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| Full Name | | Interleukin (IL)-2, human |
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| Abbreviated Name-1 | rHuIL-2; rHuIL2 |
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| Abbreviated Name-2 | Interleukin-2; Interleukin2 |
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| Description | In vitro studies performed on human cell lines demonstrate the immunoregulatory properties of IL-2 including: 1) enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human IL-2 dependent edll lines; 2) enhancement of lymphocyte cytotoxicity; 3) induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; 4) induction of interferon-gamma production.
Interleukin (IL)-2, human is a highly purified protein with a molecular weight of approximately 15,300 Da. The chemical name is des-alanyl-1, serine-125 human interleukin-2. It is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human IL-2. This recombinant form differs from native interleukin-2 in following ways: 1) it is not glycosylated; 2) the molecule has no N-terminal alanine; 3) the molecule has serine substituted for cysteine at amino acid position 125; 4) the aggregation state of molecule is likely to be different from that of native IL-2. |
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| M.W. | 15,300 Da |
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| Isoelectric Point | The main zone between 6.5-7.5 analysis by IEF |
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| Purity | Greater than 95% as determined by the following methods:
(a) SEC-HPLC analysis
(b) Reducing and non-reducing SDS-PAGE silver-stained gel analysis |
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| Endotoxin Level | Less than 0.1 ng/μg (0.1 IEU/μg) determined by LAL test |
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| Specific Activity | The specific activity as determined and was found to be greater than 1.0×107 IU/mg. |
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| Storage | Lyophilized rHuIL-2 remains stable at room temperature for three weeks, but it is best stored desiccated below -18°C. Upon reconstitution rHuIL-2 should be stored at 4°C for up to seven days. For long term storage it is recommended that a carrier protein (0.1% HSA or BSA) be added. Avoid repeated freeze-thaw cycles. |
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| Formulation | The protein (1.1 mg/ml) was lyophilized after extensive dialysis against 0.17 mg sodium monobasic and 0.89 mg dibasic sodium phosphate buffer to a pH7.5. |
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| Reconstitution | It is recommended to reconstitute the lyophilized rHuIL-2 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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| Sequence analysis | The sequence of the first fifteen N-terminal amino acids has been found to be Met-Ala-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Thr-Gln-Leu-Gln-Leu-Glu. |
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