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Recombinant Thermus thermophilus Cytochrome c oxidase subunit 1 (cbaA), partial

Recombinant Thermus thermophilus Cytochrome c oxidase subunit 1 (cbaA), partial

Code	CSB-YP732877TNT
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP732877TNT
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP732877TNT-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-BP732877TNT
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP732877TNT
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

cbaA

Uniprot No.

Q5SJ79

Alternative Names

cbaA; TTHA1135Cytochrome c oxidase subunit 1; EC 1.9.3.1; Cytochrome c ba(3) subunit I; Cytochrome c oxidase polypeptide I; Cytochrome cba3 subunit 1

Species

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Protein Length

Partial

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

Gene References into Functions

Results indicatethe importance of valine 236 (V236) in facilitating access of ligands to the active site in ba3 cytochrome oxidase. PMID: 28026953
O2 diffuses to the active site of Cytochrome ba3 exclusively via a Y-shaped hydrophobic tunnel with two 25-A long membrane-accessible branches. PMID: 26845082
Characterized is a ferrous heme a3-nitro species in ba3-cytochrome c oxidase by resonance Raman spectroscopy. This provides the first evidence for the structure of a nitrite-bound species in the binuclear heme/copper center of cytochrome c oxidases. PMID: 25406996
Thr312Val and Tyr244Phe mutations interfere with a structural rearrangement in the proton pathway that is rate limiting for proton transfer to the catalytic site. PMID: 24004023
Studies indicate that the ba(3) cytochrome c oxidase pump protons with a lower stoichiometry of 0.5 H(+)/electron and use only one proton pathway for the transfer of all protons. PMID: 22172736
Data show that a fraction of cytochrome ba(3) (ba(3)) decayed to the oxidized state within the dead time (~1ms), while the remaining amount was in a reduced state that decayed slowly to the oxidized state without accumulation of detectable intermediates. PMID: 22138627
Studies indicate that nitric oxide (NO) binding to reduced ba(3) and bovine cytochrome aa3. PMID: 22201543
Data indicate that the Crystal structures of CO-bound cytochrome ba(3)-oxidase reveal a Fe-C distance of ~2.0A, a Cu-O distance of 2.4A and a Fe-C-O angle of ~126 degrees . PMID: 22226917
Studies indicate that the ba(3)-oxidase structure has provided evolutionary and functional information. PMID: 22385645
analysis of protonation/deprotonation of tyrosine residues in cytochrome ba3 oxidase from Thermus thermophilus by time-resolved step-scan Fourier transform infrared spectroscopy PMID: 21757723
the electron transfer pathway from the heme of cytochrome c552 to the CuA center of the ba3 oxidase has been predicted PMID: 16554303