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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 E.coli O157:H7 fliP 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)
Flagellar biosynthetic protein fliPEditorial/Sponsord
EditorialUniprot ID
P0AC06Gene Names
fliPOrganism
E.coli O157:H7AASequence
QLPGITSQPLPGGGQSWSLPVQTLVFITSLTFIPAILLMMTSFTRIIIVFGLLRNALGTP SAPPNQVLLGLALFLTFFIMSPVIDKIYVDAYQPFSEEKISMQEALEKGAQPLREFMLRQ TREADLGLFARLANTGPLQGPEAVPMRILLPAYVTSELKTAFQIGFTIFIPFLIIDLVIA SVLMALGMMMVPPATIALPFKLMLFVLVDGWQLLVGSLAQSFYSExpression Region
22-245aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1538Purity
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
Biosynthetic Incorporation of Tryptophan Analogs in Proteins
Biosynthetic incorporation of Trp analogs in a protein can help in its characterization using fluorescence spectroscopy and other methodologies like NMR and phosphorescence. Here a protocol is presented resulting in the efficient
Visual Mapping of Cell Wall Biosynthesis
expression of recombinant proteins tagged with fluorescent proteins and live cell imaging with confocal laser scanning microscopy (CLSM) allows efficient visualization of biosynthetic enzymes and proteins in subcellular compartments. We have also successfully
Selective Isotopic Labeling of Recombinant Proteins Using Amino Acid Auxotroph Strains
as an expression host for selective labeling of proteins. The application of aromatic auxotroph strains of Pichia pastoris to labeling tyrosines in a recombinant protein (galactose oxidase) will be used to illustrate selective-labeling methods.
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