Recombinant Drosophila melanogaster Thioredoxin reductase 1, mitochondrial (Trxr-1), partial

Code CSB-BP310089DLU
MSDS
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Source Baculovirus
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Code CSB-EP310089DLU-B
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-MP310089DLU
MSDS
Size Pls inquire
Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Trxr-1
Uniprot No.
Alternative Names
Trxr-1; GR; CG2151; Thioredoxin reductase 1; mitochondrial; TrxR-1; EC 1.8.1.9
Species
Drosophila melanogaster (Fruit fly)
Expression Region
-
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.
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
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.

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Target Background

Function
Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.
Gene References into Functions
  1. Overexpression of mitochondrial TXNRD2 in Drosophila melanogaster extended median lifespan in female flies with a small lifespan extension in males; in contrast, overexpression of the cytosolic form, TXNRD1, did not produce a lifespan extension. PMID: 28474396
  2. Molecular orbital calculations suggested that the C-terminal hexapeptide Pro-Ala-Ser-Cys-Cys-Ser-OH functions as a redox center that alleviates the necessity for selenium in Dm-TrxR. PMID: 21389620
  3. mitochondrial and cytoplasmic variants are both essential for viability PMID: 11796729
  4. analysis of the mechanism of high Mr thioredoxin reductase from Drosophila melanogaster PMID: 12816954
  5. changing of His106 to asparagine, glutamine, and phenylalanine in various C-terminal mutants of Drosophila melanogaster thioredoxin reductase drops catalytic activity without change in pH profile PMID: 15670839
  6. X-ray crystal structure of thioredoxin reductase at 2.4 A resolution; demonstrated that tetrapeptides equivalent to the oxidized C-terminal active sites of both mouse mitochondrial TR (mTR3) and DmTR are substrates for the truncated forms of both enzymes PMID: 17385893
  7. redox potentials provide direct evidence for proposed catalytic mechanism of DmTrxR, & cast new light on essential role of DmTrx system in cycling GSSG/GSH & maintaining intracellular redox homeostasis in D. melanogaster without glutathione reductase. PMID: 17550271
  8. rates of steps in both the reductive and the oxidative half-reactions are markedly diminished in H464'Q thioredoxin reductase as compared to those of wild-type enzyme, indicating that His-464' is involved in both half-reactions PMID: 18211101
  9. the role of Glu-469' in catalysis by DmTrxR PMID: 18991392

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Subcellular Location
[Isoform B]: Mitochondrion.; [Isoform A]: Cytoplasm.
Protein Families
Class-I pyridine nucleotide-disulfide oxidoreductase family
Tissue Specificity
During embryogenesis, expression is seen in germ cell progenitors, developing midgut, hindgut and proventriculus.
Database Links

KEGG: dme:Dmel_CG2151

STRING: 7227.FBpp0071116

UniGene: Dm.20991

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