Analytical Data
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Gene name
TXNDC8
- Application
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Alternative Names
TXNDC8; SPTRX3; TRX6; Thioredoxin domain-containing Protein 8; Spermatid-specific thioredoxin-3; Sptrx-3; Thioredoxin-6
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6A555
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Expression Region
1-127 aa
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AA Sequence
MVQIIKDTNEFKTFLTAAGHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVN NSPELAETCHIKTIPTFQMFKKSQKVTLFSRIKRIICCYRSGFMSNLIFEFCGADAKKLE AKTQELM
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Molecular Weight
14.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
TXNDC8, or Thioredoxin Domain Containing 8, is a member of the thioredoxin family of proteins, which are characterized by their redox activity and involvement in various cellular processes. It has been implicated in cellular stress responses, protein folding, and the regulation of redox homeostasis. Recent studies suggest that TXNDC8 plays a crucial role in cancer biology, particularly in tumor progression and metastasis, by influencing cellular signaling pathways and the tumor microenvironment. Given its involvement in these critical processes, research into TXNDC8 recombinant proteins has gained attention in the context of therapeutic development. By isolating and characterizing TXNDC8, researchers aim to better understand its functional mechanisms and potential as a biomarker or therapeutic target in cancer and other diseases. Therefore, the study of TXNDC8 recombinant proteins can provide valuable insights into the protein's biological functions and its therapeutic potential, making it a promising candidate for future research endeavors in the fields of cancer biology and redox biology.
