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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
"-20°C/-80°C"
- 保质期：
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
- 英文名：
Customized Vaccinia virus OPG070 Protein (in vitro E.coli)
- 库存：
200
- 供应商：
武汉华美生物工程有限公司
- 规格：
20ug
Alternative Name(s)
Protein E8Editorial/Sponsord
EditorialUniprot ID
P23372Gene Names
OPG070Organism
Vaccinia virusAASequence
MAATVPRFDDVYKNAQRRILDQETFFSRGLSRPLMKNTYLFDNYAYGWIPETAIWSSRYA NLDASDYYPISLGLLKKFEFLMSLYKGPIPVYEEKVNTEFIANGSFSGRYVSYLRKFSAL PTNEFISFLLLTSIPIYNILFWFKNTQFDITKHTLFRYVYTDNAKHLALARYMHQTGDYK PLFSRLKENYIFTGPVPIGIKDINHPNLSRARSPSDYETLANISTILYFTKYDPVLMFLL FYVPGYSITTKITPAVEYLMDKLNLTKSDVQLLExpression Region
1-273aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1602Purity
Greater than 85% as determined by SDS-PAGE.Storage Buffer
Tris/PBS-based buffer, 6% TrehaloseStorage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.Endotoxin
Not Test. Endotoxin removal service is available for free upon you request.产品类型
Transmembrane-Protein备注
**产品信息可能有变动，请以官网信息为准
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文献和实验**产品信息可能有变动，请以官网信息为准
Use of the Vaccinia Virus/T7 Expression System for Studying HCV Protein Processing
/El, E1/E2, E2/p7, and p7/NS2 sites) (9 ,13 ), whereas an HCV-encoded serine proteinase located in the N-termmal one-third of the NS3 protein is responsible for four cleavages in the NS region (3/4A, 4A/4B, 4B/5A, and 5A/5B sites) (11 ,14 –16 ).
Scale-Up of recombinant virus and protein production in Stirred-Tank reactors
Stirred-tank fermentors were originally designed to perform microbial cultures (1 ). When the need arose for adequate, posttranslationally modified proteins, molecular biologists and bioprocess engineers turned to mammalian and insect cell
Preparation of Recombinant HIV-1 Gag Protein and Assembly of Virus-Like Particles In Vitro
. Here we describe a rapid method for the purification of Gag and its subsequent assembly into virus-like particles in a defined system in vitro. The purification scheme does not use affinity tags, but purifies the native protein by virtue of its high affinity
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