Recombinant-Thiol:disulfide-in
terchange-protein-DsbDdsbDThiol:disulfide interchange protein DsbD EC= 1.8.1.8 Alternative name(s): Protein-disulfide reductase; Disulfide reductase- ￥13636
- CUSABIO
- CN
- CSB-CF813318EGX
- 2025年07月14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 E.coli O6:H1 dsbD 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)
Thiol:disulfide interchange protein DsbD EC= 1.8.1.8 Alternative name(s): Protein-disulfide reductase; Disulfide reductaseEditorial/Sponsord
EditorialUniprot ID
Q8CVH5Gene Names
dsbDOrganism
E.coli O6:H1AASequence
GLFDAPGRSQFVPADQAFAFDFQQNQHDLNLTWQIKDGYYLYRKQIRITPEHAKIADVQL PQGVWHEDEFYGKSEIYRDRLTLPVTINQASAGATLTVTYQGCADAGFCYPPETKTVPLS EVVANNEASQPVSVPQQEQPTAQLPFSALWALLIGIGIAFTPCVLPMYPLISGIVLGGKQ RLSTARALLLTFIYVQGMALTYTALGLVVAAAGLQFQAALQHPYVLIGLAIVFTLLAMSM FGLFTLQLPSSLQTRLTLMSNRQQGGSPGGVFIMGAIAGLICSPCTTAPLSAILLYIAQS GNMWLGGGTLYLYALGMGLPLMLITVFGNRLLPKSGPWMEQVKTAFGFVILALPVFLLER VIGDIWGLRLWSALGVAFFGWAFITSLQAKRGWMRVVQIILLAAALVSVRPLQDWAFGAT HTAQTQTHLNFTQIKTVDELNQALVEAKGKPVMLDLYADWCVACKEFEKYTFSDPQVQKA LADTVLLQANVTANDAQDMALLKHLNVLGLPTILFFDGQGQEHPQARVTGFMDAETFSAH LRDRQPExpression Region
20-565aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1948Purity
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
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
on the surface of a protein. There are several reasons. First, sulfur has a low propensity to hydrogen bond, unlike oxygen. A consequence of this fact is that H2S is a gas under conditions that H2O is a liquid. Second, the thiol group of cysteine can react
Analysis of Global and Specific Changes in the Disulfide Proteome Using Redox 2D-PAGE
Protein cysteine sulfhydryl groups are susceptible to a number of redox-dependent modifications, including an interchange between the reduced sulfhydryl and an oxidized disulfide state. A growing body of evidence suggests that reversible
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