Recombinant-Encephalitozoon-cu
niculi-Uncharacterized-membrane-protein-ECU041080ECU041080Uncharacterized membrane protein ECU04_1080- ￥9772
- CUSABIO
- CN
- CSB-CF823415EKH
- 2025年07月13日
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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 Encephalitozoon cuniculi ECU04_1080 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)
Uncharacterized membrane protein ECU04_1080Editorial/Sponsord
EditorialUniprot ID
Q8SVT0Gene Names
ECU04_1080Organism
Encephalitozoon cuniculiAASequence
MAESVASSESLPQMKPEEPESKKSPSREAIPKDMPVVNVRDIMMYVENMEGMENKKLIPY VVYLDEQFKEIVQKRRKDARVVFIFMIAIMSMLVIGLVVCGVKLLGYLMEQKExpression Region
1-112aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1396Purity
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
Expression of Recombinant Matrix Metalloproteinases in Escherichia coli
With the advent of recombinant DNA technology, numerous systems have been utilized for the overexpression of proteins. Recombinant protein expression in Escherichia coli (E. coli) typically provides large quantities of the protein
Expression of Recombinant Membrane-Type MMPs
” (1 ) there has been much interest in the production of recombinant protein to facilitate both structural and functional analyses. The proteolytic activity of the membrane-type-1 MMP (MT1-MMP) has been studied using recombinant material produced from expression in E. coli (2 ,3 ). These data
Folding Engineering Strategies for Efficient Membrane Protein Production in E. coli
, and YidC in α-helical membrane protein biogenesis and describe a set of strains, vectors, and chaperone co-expression plasmids that can lead to significant gains in the production of recombinant membrane proteins in E. coli . Methods to quantify membrane
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