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Recombinant Escherichia coli Thiol:disulfide interchange protein DsbA (dsbA)

Recombinant Escherichia coli Thiol:disulfide interchange protein DsbA (dsbA)

Code	CSB-YP360109ENV
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP360109ENV
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP360109ENV-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP360109ENV
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP360109ENV
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

dsbA

Uniprot No.

P0AEG4

Alternative Names

dsbA; dsf; ppfA; b3860; JW3832Thiol:disulfide interchange protein DsbA

Species

Escherichia coli (strain K12)

Expression Region

20-208

Target Protein Sequence

A QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL NPQGMDTSNM DVFVQQYADT VKYLSEKK

Protein Length

Full Length of Mature Protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

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.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.

Gene References into Functions

analysis of mutants that map to two areas in the structure of DsbB, one located between the two first transmembrane segments where the quinone ring binds and the other located in the second periplasmic loop of DsbB, which interacts with DsbA PMID: 28232484
DsbA and DsbL introduce the disulfide bond into unfolded bacterial aryl sulfotransferase (ASST) at similar rates. PMID: 24601529
A high-resolution structural model of integral membrane protein DsbB in E. coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. PMID: 23416557
Studies indicate that DsbA could effectively assist proteins folding, both in vivo coexpressed with the target protein, and in vitro replenished as foldases. PMID: 17366881
Conversion of the conserved cis proline 151 of DsbA to several hydrophilic residues results in accumulation of mixed disulfides between DsbA and its dedicated oxidant, DsbB. PMID: 15687218
Results describe the crystal structure of the DsbA mutant C33A at 2.0 angstroms resolution. PMID: 15755450
These results suggest that DsbA uses not only the signal recognition particle targeting pathway but also a special route of translocation through the translocon. PMID: 15937162
Results describbe the catalytic mechanism of DsbL, and provide evidence for proton shuffling during catalysis. PMID: 18692066
Study identified cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA, a periplasmic disulfide bond-forming enzyme, are covalently linked by a disulfide bond. PMID: 19766568