| Full Name |
Interleukin-2 (IL-2), Human
|
Abbreviated Name-1 |
rHuIL-2; rHuIL2 |
| Documents |
|---|
 MSDS: 20111227043736 (PDF) |
| COA: Z00368_12372802 (PDF) |
| Figures |
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| Reference |
|---|
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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|
Abbreviated Name-2 |
Interleukin-2; Interleukin2 |
Description |
In vitro studies performed on human cell lines demonstrate the immunoregulatory properties of Interleukin-2 (IL-2) including: 1) enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human Interleukin-2 (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.
Human Interleukin-2 (IL-2) 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 Human Interleukin-2 (IL-2) gene. Genetic engineering techniques were used to modify the human Interleukin-2 (IL-2) gene, and the resulting expression clone encodes a modified human Interleukin-2 (IL-2). This recombinant form differs from native Interleukin-2 (IL-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 Interleukin-2 (IL-2). |
M.W. |
15,300 Da |
Isoelectric Point |
The main zone between 6.5-7.5 analysis by IEF |
Purity |
Greater than 98% as determined by the following methods:
(a) SEC-HPLC analysis
(b) Reducing and non-reducing SDS-PAGE silver-stained gel analysis |
Endotoxin Level |
Less than 0.1 ng/μg (1 IEU/μg) determined by LAL test |
Specific Activity |
The specific activity as determined and was found to be greater than 1.0×107 IU/mg. |
Storage |
Lyophilized Recombinant Human Interleukin-2 (IL-2) remains stable at room temperature for three weeks, but it is best stored desiccated below -18°C. Upon reconstitution Recombinant Human Interleukin-2 (IL-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. |
Formulation |
The protein was lyophilized after extensive dialysis against 50mM Phosphate buffer, pH7.5, 5% Mannitol buffer. |
Reconstitution |
It is recommended to reconstitute the lyophilized Recombinant Human Interleukin-2 (IL-2) in sterile 18 MΩ-cm H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions. |
Sequence analysis |
The sequence of the first five N-terminal amino acids has been found to be Met-Pro-Thr-Ser-Ser. |
