Recombinant Human IL-2 Protein, ≥95% (SDS-PAGE, SEC-HPLC), high purity

Features and benefits
  • Expression System: CHO-K1
  • Accession #: P60568
  • Protein Tag: His
  • Bioactivity: Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is typically <2.5ng/mL.
  • Endotoxin Concentration: <5.0 EU/mg
Item Number
rp147476
Grouped product items
SKUSizeAvailabilityPrice 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

Basic Description

Product NameRecombinant Human IL-2 Protein, ≥95% (SDS-PAGE, SEC-HPLC), high purity
SynonymsAldesleukin; IL2; IL-2; IL-2lymphokine; interleukin 2; interleukin-2; involved in regulation of T-cell clonal expansion; Proleukin; T cell growth factor; T-cell growth factor; TCGF
GradeActiBioPure™, 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 & PurityActiBioPure™, Bioactive, GMP, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE)
Purity≥95% (SDS-PAGE, SEC-HPLC)
BioactivityMeasured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is typically <2.5ng/mL.
Endotoxin Concentration<5.0 EU/mg
Expression SystemCHO-K1
SpeciesHuman
Amino Acids21-153 aa
SequenceAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT
Protein TagHis
Protein LengthFull length protein
Accession #P60568
SourceRecombinant
Predicted molecular weight15.4 kDa
SDS-PAGE13.0 kDa, under reducing conditions; 13.0 kDa, under non-reducing conditions.

Images

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.

Product Specifications

FormLyophilized
ReconstitutionIt 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 TempStore at -20°C
Shipped InIce chest + Ice pads
Stability And StorageShipped 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.

Certificates

Certificate of Analysis(COA)

Enter Lot Number to search for COA:

Find and download the COA for your product by matching the lot number on the packaging.

3 results found

Lot NumberCertificate TypeDateItem
ZJ23F0600484Certificate of AnalysisJul 03, 2023 rp147476
ZJ23F0600486Certificate of AnalysisJul 03, 2023 rp147476
ZJ23F0600485Certificate of AnalysisJul 03, 2023 rp147476

Related Documents

References

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]
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]
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]
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]

Solution Calculators