Product Details

Purity

>85% (SDS-PAGE)

Target Names

TRX1

Uniprot No.

P22217

Alternative Names

TRX1; TRX2; YLR043C; Thioredoxin-1; Thioredoxin I; TR-I; Thioredoxin-2

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Expression Region

2-103

Target Protein Sequence

VTQFKTASE FDSAIAQDKL VVVDFYATWC GPCKMIAPMI EKFSEQYPQA DFYKLDVDEL GDVAQKNEVS AMPTLLLFKN GKEVAKVVGA NPAAIKQAIA ANA

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.

Target Background

Function

Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism.

Gene References into Functions

NMR spectroscopic studies of yeast TRX1 provide insights into the mechanism for the closing of the water cavity. PMID: 26482062
TRX1 is required to maintain the IMS small Tim proteins in reduced forms and facilitate their mitochondrial import PMID: 22878414
Results show that an oxidized sulfiredoxin under disulfide state is formed between the catalytic Cys(84) and Cys(48), and this oxidized is reduced selectively by thioredoxin. PMID: 19801666
The cytosolic form of thioredoxin Trx1 has been cloned, expressed, purified and crystallized. PMID: 18391437
Human wt p53 expression in yeast leads to gene repression of thioredoxin (TRX1/2), a highly conserved multifunctional antioxidative and antiapoptotic protein family. PMID: 19054132
X-ray diffraction analysis of glutathionylated Trx1 C33S mutant from yeast PMID: 19153453
study solved the crystal structures of oxidized Trx1 and glutathionylated Trx1Cys33Ser mutant at 1.76 and 1.80 A, respectively; kinetic studies proved that Met35Arg mutation could alter the apparent K(m) and V(max) values of the reaction PMID: 19362171
Trx1 and Trx2 are essential for the nuclear accumulation of Msn2/4 and Maf1. PMID: 19581440

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Subcellular Location

Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Mitochondrion intermembrane space.

Protein Families

Thioredoxin family

Database Links

KEGG: sce:YLR043C

STRING: 4932.YLR043C

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Code	CSB-YP325248SVG
MSDS	MSDS
Size	Pls inquire
Source	Yeast
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-EP325248SVG
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP325248SVG-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-BP325248SVG
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP325248SVG
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Recombinant Saccharomyces cerevisiae Thioredoxin-1 (TRX1)

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