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Recombinant Human IFN-alpha-2B Protein

功能和特点
  • 规格或纯度: Animal Free, >98% ( SDS-PAGE and HPLC), Active, Yeast, No tag, 24-188 aa
  • 生物活性: Fully biologically active when compared to standard. The specific activity determined by an anti-viral assay is no less than 1.6 × 10^8 IU/mg.
  • 蛋白标签: No tag
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库存信息

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库存信息

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货号 (SKU) 包装规格 是否现货 价格 数量
rp156087-10μg
10μg 期货 Stock Image
rp156087-100μg
100μg 现货 Stock Image
rp156087-1mg
1mg 期货 Stock Image

基本描述

产品名称 Recombinant Human IFN-alpha-2B Protein
英文别名 IFN-alpha-2 | Interferon alpha-A | LeIF A
规格或纯度 Animal Free, >98% ( SDS-PAGE and HPLC), Active, Yeast, No tag, 24-188 aa
产品介绍

干扰素(IFN)以其在宿主防御机制中的关键作用而闻名。Ⅰ型干扰素包括IFN-alpha 家族,IFN-beta, -omega,-kappa 和 Limitin/IFN-zeta,对调节病毒感染的免疫应答具有重要意义。Ⅱ型干扰素组仅包括干扰素γ。IFN-γ是一种多功能细胞因子,具有抗增殖、免疫调节和促炎症作用,对免疫应答的许多方面都很重要。Ⅲ型干扰素家族包括IL-29/IFN-lambda 1, IL-28A/IFN-lambda 2, IL-28B/IFN-lambda 3, and IFN-lambda 4。与Ⅰ型干扰素类似,Ⅲ型干扰素具有抗病毒、抗增殖和免疫调节作用。

IFN-αs are proteins secreted by leukocyte. They are mainly involved in innate immune response against viral infection. The IFN-α family has 13 subtypes and 23 different variants. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

生物活性 Fully biologically active when compared to standard. The specific activity determined by an anti-viral assay is no less than 1.6 × 10^8 IU/mg.
表达系统 Yeast
种属 Human
氨基酸 24-188 aa
序列 CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE
纯度 >98% ( SDS-PAGE and HPLC)
蛋白标签 No tag
蛋白长度 Full length protein
无载体
无动物源
Accession # P01563
来源 Recombinant
预测分子量 19.3 kDa

产品规格参数

物理外观 Lyophilized
储存缓冲液 Lyophilized from a 0.2 µm filtered solution in 1×PBS, pH 7.4, with 0.02 % Tween-20.
复溶 We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportio
储存温度 -20°C储存,避免反复冻融
运输条件 超低温冰袋运输
稳定性与储存 Upon delivery aliquot, Store at -20°C, Avoid freeze / thaw cycles. Lyophilized with no additives. This product is an active protein and may elicit a biological response in vivo, handle with caution.

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图片

Recombinant Human IFN-alpha-2B Protein (rp156087)-Protein Bioactivity
Fully biologically active when compared to standard. The specific activity determined by an anti-viral assay is no less than 1.6×10⁸ IU/mg.

Recombinant Human IFN-alpha-2B Protein (rp156087)-SDS-PAGE
Recombinant Human IFN-alpha-2B 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 19.3 kDa under reducing conditions and 16.2 kDa under non-reducing conditions.


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FAQ
巨噬细胞刺激蛋白(MSP)
巨噬细胞刺激蛋白(MSP)
Macrophage Stimulating Protein (MSP)

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参考文献

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13. Klaus, W W, Gsell, B B, Labhardt, A M AM, Wipf, B B and Senn, H H..  (1997)  The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution..  Journal of molecular biology,    (12):  ().  [PMID:9417943]
14. Nyman, T A TA, Tölö, H H, Parkkinen, J J and Kalkkinen, N N..  (1998)  Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes..  The Biochemical journal,    (15):  ().  [PMID:9425112]
15. Austruy, E E and 7 more authors..  ()  A defective retroviral vector encoding human interferon-alpha2 can transduce human leukemic cell lines..  Cancer gene therapy,    ():  ().  [PMID:9694076]
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18. Quadt-Akabayov, Sabine R SR, Chill, Jordan H JH, Levy, Rina R, Kessler, Naama N and Anglister, Jacob J..  (2006)  Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex..  Protein science : a publication of the Protein Society,    ():  ().  [PMID:17001036]
19. Gull, Iram I, Samra, Zahoor Qadir ZQ, Aslam, Muhammad Shahbaz MS and Athar, Muhammad Amin MA..  (2013)  Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b..  SpringerPlus,    ():  ().  [PMID:23875128]