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Recombinant Human Thioredoxin/TXN

Recombinant Human Thioredoxin/TXN Recombinant Human Thioredoxin/TXN

Instruction Manual!

Product name: Recombinant Human Thioredoxin/TXN
Source:E. coli
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,PH7.2.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source E. coli
Description Recombinant Human Thioredoxin is produced by our E.coli expression system and the target gene encoding Met1-Val105 is expressed with a 6His tag at the N-terminus.
Names Thioredoxin, Trx, ATL-Derived Factor, ADF, Surface-Associated Sulphydryl Protein, SASP, TXN, TRDX, TRX, TRX1
Accession # P10599
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,PH7.2.
Shipping The product is shipped at ambient temperature.
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
MGSSHHHHHHSSGLVPRGSHMVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSL SEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
Background Thioredoxin (TXN) is a member of the Thioredoxin family. Thioredoxin exists as a disulfide-linked homodimer and contains one Thioredoxin domain. Thioredoxin is up-regulated by ionizing radiation. Thioredoxin participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin also plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide.

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