| SKU | Size | Availability | Price | Qty |
|---|---|---|---|---|
| rp147476-10μg | 10μg | Available within 4-8 weeks(?) Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience! | $59.90 | |
| rp147476-50μg | 50μg | Available within 4-8 weeks(?) Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience! | $139.90 | |
| rp147476-100μg | 100μg | Available within 4-8 weeks(?) Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience! | $229.90 | |
| rp147476-1mg | 1mg | Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding. | $699.90 |
GMP, ≥95% (SDS-PAGE, SEC-HPLC), Active, CHO-K1, His, 21-153 aa
| Product Name | Recombinant Human IL-2 Protein, ≥95% (SDS-PAGE, SEC-HPLC), high purity |
|---|---|
| Synonyms | IL-2 | T-cell growth factor | TCGF |
| Grade | ActiBioPure™, Azide Free, Bioactive, Carrier Free, GMP, High Performance |
| Product Description | Purity ≥95% (SDS-PAGE, SEC-HPLC) Additional sequence information 133 amino acids Function Interleukin-2, or interleukin-2, is also known as T cell growth factor (TCRF). A wide range of bioactive cytokines produced primarily by activated CD4+T cells and CD8+T cells. It is a growth factor of all T cell subsets, which can make T cells survive in vitro for a long time and promote the proliferation of activated B cells. Therefore, it is an important factor in the regulation of immune response, and also involved in antibody response, hematopoietic and tumor surveillance. Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. This product is a recombinant protein expressed by eukaryotic cells. The protein gene was inserted into stable expression vector and transformed into CHO-K1 cells. After cloning, screening and quality verification, the selected stable expression strain was prepared by fermentation of the medium determined by chemical composition (without any animal source components). This product is a sterile lyophilized powder, made from a protein solution containing 10mM phosphate with a pH of 7.2 filtered by 0.2μm. |
| Specifications & Purity | ActiBioPure™, Bioactive, GMP, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE) |
| Purity | ≥95% (SDS-PAGE, SEC-HPLC) |
| Bioactivity | 1、Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is typically less than 2.5 ng/mL. 2、Measured in a cell proliferation assay using mouse splenocytes. The ED50 for this effect is typically less than 30 |
| Endotoxin Concentration | <1.0 EU/μg |
| Expression System | CHO-K1 |
| Species | Human |
| Amino Acids | 21-153 aa |
| Sequence | APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT |
| Protein Tag | His |
| Protein Length | Full length protein |
| Accession # | P60568 |
| Source | Recombinant |
| Predicted molecular weight | 15.4 kDa |
| SDS-PAGE | 13.0 kDa, under reducing conditions; 13.0 kDa, under non-reducing conditions. |
Recombinant Human IL-2 Protein (rp147476)-Protein Bioactivity
Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED₅₀
for this effect is typically <2.5ng/mL.
Recombinant Human IL-2 Protein (rp147476) -SDS-PAGE
3μg/lane of Recombinant Human IL-2 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a single band at 13.0 kDa.
Recombinant Human IL-2 Protein (rp147476) - Protein Bioactivity
Measured in a cell proliferation assay using mouse splenocytes. The ED50 for this effect is typically less than 30.0 ng/mL.
| Form | Lyophilized |
|---|---|
| Reconstitution | It is recommended to dissolve the lyophilized rhIL-2 in water for injection or sterilized ultra-pure water with a concentration of not less than 100μg/ml for further dilution to working concentration. Avoid repeated freeze-thaw as much as possible. Rediss |
| Storage Temp | Store at -20°C |
| Shipped In | Ice chest + Ice pads |
| Stability And Storage | Shipped at 4°C. Store at -20°C. Lyophilized with no additives. This product is an active protein and may elicit a biological response in vivo, handle with caution. |
Enter Lot Number to search for COA:
Find and download the COA for your product by matching the lot number on the packaging.
| Lot Number | Certificate Type | Date | Item |
|---|---|---|---|
 ZJ23F0600484 | Certificate of Analysis | Jul 03, 2023 | rp147476 |
| ZJ23F0600486 | Certificate of Analysis | Jul 03, 2023 | rp147476 |
| ZJ23F0600485 | Certificate of Analysis | Jul 03, 2023 | rp147476 |
| 1. Quéméner A, Maillasson M, Arzel L, Sicard B, Vomiandry R, Mortier E, Dubreuil D, Jacques Y, Lebreton J, Mathé-Allainmat M. (2017) Discovery of a Small-Molecule Inhibitor of Interleukin 15: Pharmacophore-Based Virtual Screening and Hit Optimization.. J Med Chem, 60 (14): (6249-6272). [PMID:28657314] [10.1021/op500134e] |
| 2. Chen L, Du J, Dai Q, Zhang H, Pang W, Hu J.. (2014) Prediction of anti-tumor chemical probes of a traditional Chinese medicine formula by HPLC fingerprinting combined with molecular docking.. Eur J Med Chem, 83 (294-306). [PMID:24974349] [10.1016/j.ejmech.2014.06.037] |
| 3. Żyżyńska-Granica B, Trzaskowski B, Niewieczerzał S, Filipek S, Zegrocka-Stendel O, Dutkiewicz M, Krzeczyński P, Kowalewska M, Koziak K.. (2017) Pharmacophore guided discovery of small-molecule interleukin 15 inhibitors.. Eur J Med Chem, 136 (543-547). [PMID:28535470] [10.1016/j.ejmech.2017.05.034] |
| 4. Laâbi, Y Y and 6 more authors.. (1992) A new gene, BCM, on chromosome 16 is fused to the interleukin 2 gene by a t(4;16)(q26;p13) translocation in a malignant T cell lymphoma.. The EMBO journal, [PMID:1396583] |
| 5. Mott, H R HR and 5 more authors.. (1992) Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.. Biochemistry, (25): [PMID:1510960] |
| 6. and Bazan, J F JF.. (1992) Unraveling the structure of IL-2.. Science (New York, N.Y.), (17): [PMID:1631562] |
| 7. Conradt, H S HS and 5 more authors.. (1989) Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells. Structure of O-linked carbohydrate chains and their location within the polypeptide.. The Journal of biological chemistry, (15): [PMID:2793860] |
| 8. Weir, M P MP, Chaplin, M A MA, Wallace, D M DM, Dykes, C W CW and Hobden, A N AN.. (1988) Structure-activity relationships of recombinant human interleukin 2.. Biochemistry, (6): [PMID:3264184] |
| 9. Siebenlist, U U and 7 more authors.. (1986) Promoter region of interleukin-2 gene undergoes chromatin structure changes and confers inducibility on chloramphenicol acetyltransferase gene during activation of T cells.. Molecular and cellular biology, [PMID:3491296] |
| 10. Brandhuber, B J BJ, Boone, T T, Kenney, W C WC and McKay, D B DB.. (1987) Three-dimensional structure of interleukin-2.. Science (New York, N.Y.), (18): [PMID:3500515] |
| 11. Devos, R R and 7 more authors.. (1983) Molecular cloning of human interleukin 2 cDNA and its expression in E. coli.. Nucleic acids research, (11): [PMID:6306584] |
| 12. Maeda, S S and 9 more authors.. (1983) Cloning of interleukin 2 mRNAs from human tonsils.. Biochemical and biophysical research communications, (30): [PMID:6312994] |
| 13. Fujita, T T, Takaoka, C C, Matsui, H H and Taniguchi, T T.. (1983) Structure of the human interleukin 2 gene.. Proceedings of the National Academy of Sciences of the United States of America, [PMID:6324170] |
| 14. Holbrook, N J NJ, Lieber, M M and Crabtree, G R GR.. (1984) DNA sequence of the 5' flanking region of the human interleukin 2 gene: homologies with adult T-cell leukemia virus.. Nucleic acids research, (25): [PMID:6330695] |
| 15. Robb, R J RJ, Kutny, R M RM, Panico, M M, Morris, H R HR and Chowdhry, V V.. (1984) Amino acid sequence and post-translational modification of human interleukin 2.. Proceedings of the National Academy of Sciences of the United States of America, [PMID:6333684] |
| 16. Taniguchi, T T and 6 more authors.. (1983) Structure and expression of a cloned cDNA for human interleukin-2.. Nature, [PMID:6403867] |
| 17. Holbrook, N J NJ and 5 more authors.. (1984) T-cell growth factor: complete nucleotide sequence and organization of the gene in normal and malignant cells.. Proceedings of the National Academy of Sciences of the United States of America, [PMID:6608729] |
| 18. Bamborough, P P, Hedgecock, C J CJ and Richards, W G WG.. (1994) The interleukin-2 and interleukin-4 receptors studied by molecular modelling.. Structure (London, England : 1993), (15): [PMID:7529123] |
| 19. Eizenberg, O O, Faber-Elman, A A, Lotan, M M and Schwartz, M M.. (1995) Interleukin-2 transcripts in human and rodent brains: possible expression by astrocytes.. Journal of neurochemistry, [PMID:7722480] |
| 20. Miyazaki, T T and 9 more authors.. (1994) Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits.. Science (New York, N.Y.), (11): [PMID:7973659] |
| 21. Chernicky, C L CL, Tan, H H, Burfeind, P P, Ilan, J J and Ilan, J J.. (1996) Sequence of interleukin-2 isolated from human placental poly A+ RNA: possible role in maintenance of fetal allograft.. Molecular reproduction and development, [PMID:8824916] |
| 22. Wang, Xinquan X, Rickert, Mathias M and Garcia, K Christopher KC.. (2005) Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.. Science (New York, N.Y.), (18): [PMID:16293754] |
| 23. Stauber, Deborah J DJ, Debler, Erik W EW, Horton, Patricia A PA, Smith, Kendall A KA and Wilson, Ian A IA.. (2006) Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.. Proceedings of the National Academy of Sciences of the United States of America, (21): [PMID:16477002] |
| 24. Fiebich, Bernd L BL and 6 more authors.. (2012) Pseudoephedrine inhibits T-cell activation by targeting NF-κB, NFAT and AP-1 signaling pathways.. Immunopharmacology and immunotoxicology, [PMID:21631396] |
