Analytical Data
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Gene name
CNX
- Application
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Alternative Names
CANX; CNX; IP90; P90; Major Histocompatibility Complex Class I Antigen-Binding Protein p88
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35564
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Expression Region
Leu263~Pro482
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Molecular Weight
50kDa
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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 study of CNX (calnexin) recombinant proteins is rooted in the understanding of the endoplasmic reticulum (ER) quality control system, which plays a vital role in protein folding and maturation. Calnexin is a chaperone protein that assists in the proper folding of glycoproteins within the ER, ensuring that only correctly folded proteins proceed to the next stage of the secretory pathway. Given its central role in maintaining cellular homeostasis, research into CNX has significant implications for understanding diseases related to protein misfolding, such as neurodegenerative disorders and certain cancers. The recombinant form of CNX enables researchers to investigate its structure-function relationships, as well as its interactions with other proteins during the folding process. This research is crucial, not only for elucidating the molecular mechanisms underlying protein quality control but also for developing therapeutic strategies that target CNX for diseases where protein misfolding is a contributing factor. By producing and analyzing CNX recombinant proteins, scientists can explore potential applications in biotechnology and pharmacology, aiming to manipulate the protein's functions or improve its biotechnological applications in protein production and therapeutic development. Overall, the investigation of CNX recombinant proteins is a significant step toward advancing our knowledge in cell biology and disease treatment.
