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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
2-8°C
- 保质期:
1年
- 英文名:
HIV Type-O Envelope
- 库存:
999
- 供应商:
南京赛泓瑞
- 规格:
/5ug/20ug/1mg
Recombinant Measles Virus (399-525)
英文简称:
Measles (399-525)
中文名称:
重组麻疹病毒(399-525)
背景资料:
Measles, also known as rubeola, caused by a virus, specifically a paramyxovirus of the genus Morbillivirus. To date, 21 strains of the measles virus have bThe E. Coli derived recombinant protein contains the large fusion protein immunodominant regions, 399-525 amino acids.n identified. Measles virus (MV) is an enveloped, nonsegmented negative-stranded RNA virus of the Paramyxoviridae family.
产品描述:
The E. Coli derived recombinant protein contains the large fusion protein immunodominant regions, 399-525 amino acids.
来源宿主:
大肠杆菌中重组表达
序列:
溶解建议:
提供的重组麻疹病毒(399-525)产品为溶液形式.该产品已溶解在含60mM NaCl, 10mM 谷胱甘肽和50%甘油的50mM Tris-HCl缓冲液(pH 8.0).
保存建议:
Five years frozen. One month in solution at room temperature.
其他简介:
ProSpec是一家全球著名细胞因子蛋白及相关抗体生产和研发品牌。ProSpec的生产和研发工厂位于以色列,专注于蛋白(重组及合成)生产研发,其独有的细菌和哺乳动物表达和蛋白折叠技术使其能在17年内成长为国际的科研级蛋白供应商。目前ProSpec可以提供细胞因子,生长因子,激素,信号蛋白,病毒抗原等近800种重组蛋白和100多种抗体,是世界上提供蛋白品种最多的公司之一,领先的生产工艺和规模使其可以提供毫克到克级蛋白,价格优于同类公司。绝大部分产品是天然成熟型蛋白,而不含有标签蛋白。考虑到大部分研究者希望能更灵活地配制蛋白溶液,ProSpec-Tany绝大部分产品没有添加保护剂或盐,这就对工艺提出了更高的要求。同时,ProSpec-Tany绝大部分产品为冻干粉,因此易于运输和保存。
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文献和实验Expression of EGF and HIV Envelope Glycoprotein
This chapter reviews the expression of two proteins that are naturally secreted: murine epidermal growth factor (mEGF) and the 120-kDa envelope protein from human immunodeficiency virus (HIV-1 ENV). Although the initial aims of these projects
Use of Lectins in Affinity Purification of HIV and SIV Envelope Glycoproteins
The human immunodeficiency viruses (HIV-1 and HIV-2) are the etiologic agents of the acquired immunodeficiency syndrome (AIDS) and related disorders (1 -3 ) Simian immunodeficiency virus(SIV) is the corresponding virus
Characterization of HIV gp120 Envelope Glycoprotein by Lectin Analysis
The envelope glycoprotein gp120 of the human immunodeficiency virus (HIV), the causative agent of AIDS, contains approx 24 potential sites for N -glycosylation (Asn-X-Ser/Thr, X≠Pro) (1 ), all of which are utilized
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