Analytical Data
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Gene name
CNPY3/PRAT4A
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简介
The CNPY3/PRAT4A protein is a Toll-like receptor (TLR)-specific co-chaperone of HSP90B1 and is essential for the correct folding and exit of TLRs (excluding TLR3) from the endoplasmic reticulum. CNPY3/PRAT4A is critical for innate and adaptive immune responses, interacts with HSP90B1, and is destroyed in the presence of ATP. CNPY3/PRAT4A Protein, Mouse (HEK293, Fc) is the recombinant mouse-derived CNPY3/PRAT4A protein, expressed by HEK293 , with C-hFc labeled tag.
- Application
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Alternative Names
Protein canopy homolog 3; Protein associated with Tlr4; PRAT4A; TNRC5
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Species
Mouse
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9DAU1-1
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Expression Region
A27-P272
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Protein Length
Partial
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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
CNPY3, also known as PRAT4A, is a protein that has garnered attention in the field of cellular and molecular biology due to its potential involvement in various biological processes, including cell signaling and protein homeostasis. Initially identified as a co-chaperone associated with heat shock proteins, CNPY3/PRAT4A has been implicated in the regulation of the endoplasmic reticulum (ER) stress response, suggesting that it may play a crucial role in maintaining cellular proteostasis. Recent studies indicate that CNPY3 interacts with a range of client proteins and may influence their folding and stability, thus impacting overall protein quality control mechanisms within the cell. Furthermore, aberrations in CNPY3/PRAT4A expression have been linked to several diseases, including cancer and neurodegenerative disorders, emphasizing its significance in health and disease. The recombinant production of CNPY3/PRAT4A allows for in-depth investigations into its structural and functional properties, paving the way for a better understanding of its role in cellular functions and its potential as a therapeutic target. These studies are critical not only for elucidating the mechanisms underlying cellular stress responses but also for exploring innovative strategies to manipulate CNPY3 function in clinical settings. Overall, research on CNPY3/PRAT4A represents a promising frontier in the search for new insights into the intricate network of protein interactions and their implications for human health.
