Analytical Data
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Gene name
TXNDC15
- Application
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Alternative Names
TXNDC15；C5orf14；Thioredoxin domain-containing Protein 15
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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
Q96J42
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Expression Region
33-321aa
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AA Sequence
VEVAEESGRLWSEEQPAHPLQVGAVYLGEEELLHDPMGQDRAAEEANAVL GLDTQGDHMVMLSVIPGEAEDKVSSEPSGVTCGAGGAEDSRCNVRESLFS LDGAGAHFPDREEEYYTEPEVAESDAAPTEDSNNTESLKSPKVNCEERNI TGLENFTLKILNMSQDLMDFLNPNGSDCTLVLFYTPWCRFSASLAPHFNS LPRAFPALHFLALDASQHSSLSTRFGTVAVPNILLFQGAKPMARFNHTDR TLETLKIFIFNQTGIEAKKNVVVTQADQIGPLPSTLIKSVDHHHHHH
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Molecular Weight
33 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
The TXNDC15 protein is a member of the thioredoxin domain-containing family and has garnered increasing interest in recent years due to its potential role in cellular stress responses and redox regulation. As a thioredoxin-like protein, TXNDC15 is thought to participate in maintaining protein homeostasis and modulating oxidative stress, which are critical for cellular function and survival. Research has indicated that TXNDC15 may be involved in various physiological processes, including cytoprotection, metabolism, and inflammation, making it a candidate for studies in disease mechanisms, particularly in cancer and neurodegeneration. Additionally, TXNDC15’s interactions with other cellular proteins suggest its significance in signaling pathways that regulate apoptosis and cellular growth. Given its emerging roles, researchers have begun to explore the therapeutic potential of TXNDC15-targeted interventions, highlighting the importance of understanding its structure and function. The characterization and study of its recombinant form could provide essential insights into its biological activities and interactions, opening new avenues for drug development and therapeutic strategies aimed at diseases linked to oxidative stress and misfolded proteins.
