为了获得访问"阿拉丁铁蛋"实时聊天框的流畅支持体验,建议您使用Chrome浏览器或选择360浏览器极速模式(如何切换极速模式?),感谢您选择我们!

Recombinant Human IL-2 Protein

功能和特点
  • 规格或纯度: GMP, ≥95% (SDS-PAGE, SEC-HPLC), Active, CHO-K1, His, 21-153 aa
  • 生物活性: Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is typically <2.5ng/mL.
  • 蛋白标签: His
有货

库存信息

关闭

库存信息

关闭

库存信息

关闭

库存信息

关闭
货号 (SKU) 包装规格 是否现货 价格 数量
rp147476-10μg (试用装)
申请此免费试用装(?)
作为尊贵的客户,您每年可免费申请一次试用装产品,尽享探索与享受!
10μg 现货 Stock Image
rp147476-50μg
50μg 现货 Stock Image
rp147476-100μg
100μg 现货 Stock Image
rp147476-1mg
1mg 期货 Stock Image

基本描述

产品名称 Recombinant Human IL-2 Protein
别名 重组人白细胞介素-2蛋白
英文别名 IL-2 | T-cell growth factor | TCGF
规格或纯度 GMP, ≥95% (SDS-PAGE, SEC-HPLC), Active, CHO-K1, His, 21-153 aa
产品介绍


白介素2即白细胞介素-2(interleukin-2,IL-2),又名T细胞生长因子(T cell growth factor,TCRF)。主要由活化的CD4+T细胞和CD8+T细胞产生的具有广泛生物活性的细胞因子。是所有T细胞亚群的生长因子,能使T细胞在试管内长期存活,并可促进活化B细胞增殖,故为调控免疫应答的重要因子,也参与抗体反应、造血和肿瘤监视。 

本产品由真核细胞表达的重组蛋白,是将蛋白基因接入稳定表达载体,转化CHO-K1细胞,经克隆筛选,质量验证,挑选的稳定表达株,由化学成分确定的培养基(不含有任何动物源成分)发酵制备,工艺稳定,保证了产品质量及批次间的一致性。

本产品为无菌冻干粉剂,由含有 10mM 磷酸盐pH为 7.2的蛋白溶液经0.2μm过滤后分装冻干。


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.


生物活性 Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is typically <2.5ng/mL.
表达系统 CHO-K1
种属 Human
氨基酸 Amino acids
序列 APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT
纯度 ≥95% (SDS-PAGE, SEC-HPLC)
蛋白标签 His
蛋白长度 Full length protein
无载体
Accession # P60568
来源 Recombinant
预测分子量 15.4 kDa
SDS-PAGE 13.0 kDa, under reducing conditions; 13.0 kDa, under non-reducing conditions.

产品规格参数

物理外观 Lyophilized
储存缓冲液 含有 10mM 磷酸盐pH为 7.2的蛋白溶液经0.2μm过滤后分装冻干
复溶 建议将冻干 rhIL-2溶解在注射用水或灭菌的超纯水中,浓度不低于100μg/ml,以待进一步稀释至工作浓度。尽可能避免反复冻融。 复溶后的细胞因子:4℃可稳定储存7-10天;短期保存请分装后存放于-20℃。
储存温度 -20°C储存
运输条件 超低温冰袋运输
稳定性与储存 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.

质检证书(COA)

质检报告(COA)

输入批号以搜索COA:

图片

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.

相关文档

质检报告COA

请输入批号:


产品问答

产品问答

登录提交问题 Hover me 请先登录再提交问题
您提交该产品问题后,我们会在1-2个工作日内给您答复,您可以登录"我的账号",然后点击"我的产品问答"查看答案

参考文献

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]