Analytical Data
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Gene name
TXNDC4
- Application
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Alternative Names
Endoplasmic reticulum resident Protein 44. ER Protein 44. ERp44. Thioredoxin domain-containing Protein 4
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BS26
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Expression Region
1-406 aa
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AA Sequence
EITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLAPSEYRYTLLRDRDEL
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Molecular Weight
67.21 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
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Protein Description
TXNDC4, or Thioredoxin Domain Containing 4, is a member of the thioredoxin superfamily, which plays crucial roles in various cellular processes, including redox regulation, protein folding, and stress response. Research into TXNDC4 has gained traction due to its involvement in multiple biological functions and its potential implications in disease pathways, particularly in cancer and neurodegenerative disorders. The protein is known to interact with other cellular components and contributes to the maintenance of cellular homeostasis. Recent studies have indicated that TXNDC4 may participate in regulating cellular signaling pathways and modulating oxidative stress responses, which are vital for cell survival and function. Furthermore, its expression levels have been correlated with poor prognosis in certain cancer types, underscoring the need for a deeper understanding of its molecular mechanisms. Investigating TXNDC4 as a recombinant protein provides a valuable opportunity to elucidate its biochemical properties, functionality, and interactions in a controlled environment. By exploring its structural characteristics and biological activity, researchers aim to define its role in physiological and pathological contexts, potentially providing new insights for therapeutic interventions. Overall, the study of TXNDC4 represents a promising avenue for uncovering novel mechanisms of action in cellular biology and disease progression.
