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- 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 Marinobacter nauticus dsbB 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)
Disulfide bond formation protein B Alternative name(s): Disulfide oxidoreductaseEditorial/Sponsord
EditorialUniprot ID
A1TXV0Gene Names
dsbBOrganism
Marinobacter nauticusAASequence
MTSRWIFGLVFLVCAGLLAVAFYMEHVMGLEPCPLCWLQRFGFMGAGLVSLLAFLHGPRG FGNRVYGLLLIVAAGAGLAVAGRQLWLQSLPADQVPACGPSVDYMLEVLPWFEVLQTALK GTGDCAEVVWRFLGLSIPGWTAVFFSLLIVLGLFVMLRRYSPRDWLQSExpression Region
1-168aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1468Purity
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
Many proteins secreted to the bacterial cell envelope contain cysteine residues that are involved in disulfide bonds. These disulfides either play a structural role, increasing protein stability, or reversibly form in the catalytic site
Periplasmic Chaperones Used to Enhance Functional Secretion of Proteins in E. coli
milieu of the bacterial periplasm in principle enables disulfide bond formation, resulting in a correctly folded and soluble protein. However, this process often occurs at low efficiency, depending on the nature of the recombinant gene product
Recombinant Protein Expression in the Baculovirus-Infected Insect Cell System
disulfide-bond formation are necessary for protein folding and activity. Among the eukaryotic expression systems, the baculovirus-infected insect cell platform has gained particular attention, resulting in the development
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