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Recombinant Pseudomonas aeruginosa Azurin (azu)

Recombinant Pseudomonas aeruginosa Azurin (azu)

Code	CSB-YP360518EZX
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP360518EZX
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP360518EZX-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-BP360518EZX
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP360518EZX
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

azu

Uniprot No.

P00282

Alternative Names

azu; PA4922; Azurin

Species

Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Expression Region

21-148

Target Protein Sequence

AECSVDIQGN DQMQFNTNAI TVDKSCKQFT VNLSHPGNLP KNVMGHNWVL STAADMQGVV TDGMASGLDK DYLKPDDSRV IAHTKLIGSG EKDSVTFDVS KLKEGEQYMF FCTFPGHSAL MKGTLTLK

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

■ Customer Reviews

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Target Background

Function

Transfers electrons from cytochrome c551 to cytochrome oxidase.

Gene References into Functions

Review of activity of Pseudomonas aeruginosa azurin and azurin-like bacteriocins; including hijacking of key cellular regulators and cell surface receptors to remodel the cellular signaling networks. PMID: 28960574
this study shows that addition of Cys at position 78 modulates the functional shifting of this protein from a peroxidase to a chaperone PMID: 27457208
Mercury metallation of the bacterial copper protein azurin is analogous to the one of human cerulopsmin and factor VIII in mercury poisoning. PMID: 25265377
Study presents the high-resolution (1.5 A) structure of azurin from Pseudomonas aeruginosa PAO1 spin labelled with MTSSL at position T21; due to the crystal-packing environment in the triclinic crystals, the label is observed in two different but fully ordered states. PMID: 24884565
Results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function. PMID: 23911566
The study examines the spectral properties of tryptophan radicals in two azurin mutants (Az48W and ReAz108W). PMID: 23458492
Atomic force spectroscopy was used to investigate the interaction of p28 peptide fragment of azurin with full-length p53 and its isolated domains at the single molecule level. PMID: 22162658
structure of the active-site loop has a dramatic effect on the kinetic stability and the unfolding pathway PMID: 22446157
Studies indicate that in the crystal structure of azurin the H20 is strongly hydrogen bonded to Y48 (2.7-2.8A tyrosine-O to histidine-N distance. PMID: 22210190
Data show that almost all of the azurin variant potentials were shifted to higher values than WT azurin. PMID: 20615551
biophysical analysis of azurin conformational changes PMID: 15345565
Novel atomic displacement factors calculated from X-ray data from crystalline wild-type azurin indicate that residue 62 has a relative high mobility at elevated temperatures, while residue 74 is not very mobile and may act as an anchor for residue 62. PMID: 15449946
Unfolding of the beta-barrel in azurin is associated with dislocation of its unique alpha-helix with respect to the protein scaffold. PMID: 15581373
Pseudomonas aeruginosa azurin binds to tumor-suppressor protein p53 PMID: 15913547
The dramatic difference in kinetic-folding behavior between apo- and zinc-forms of azurin is rationalized in terms of small changes on a common broad activation barrier PMID: 16042382
Binding of azurin molecules to gold nanoparticle surface results in the red shift of the nanoparticle resonance plasmon band and in the quenching of the azurin single tryptophan fluorescence signal. PMID: 18938024