Analytical Data
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Gene name
CaN
- Application
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Alternative Names
PPP3CA; PPP3-CA; CCN1; CNA1; CALN; CALNA1; PP2B; PP2-B; Protein Phosphatase 3(formerly 2B),Catalytic Subunit,Alpha Isoformprotein Phosphatase 2B; Calcineurin A Alpha
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Species
Human
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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
Q08209
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Expression Region
Ile7~Ser301
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Molecular Weight
39kDa
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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 CaN (calmodulin-dependent protein phosphatase 2B) recombinant proteins has gained significant attention due to its crucial role in calcium signaling pathways and various cellular processes. CaN is a serine/threonine phosphatase that is activated by the calcium-bound form of calmodulin, playing an essential role in modulating numerous substrates, including transcription factors, ion channels, and structural proteins. Dysregulation of CaN activity is implicated in a variety of pathophysiological conditions, such as neurodegenerative diseases, cardiac hypertrophy, and autoimmune disorders. To better understand its mechanisms and interactions, researchers have focused on the production of recombinant CaN proteins. These recombinant forms allow for the controlled study of enzymatic activity, substrate specificity, and regulatory mechanisms in vitro. Innovations in molecular cloning, expression systems, and purification techniques have facilitated the generation of high-quality CaN variants that can be utilized in experimental and therapeutic settings. Moreover, the structural characterization of CaN through techniques like X-ray crystallography has provided insights into its functional domains and binding interfaces, paving the way for the development of specific inhibitors or modulators that may serve as potential therapeutic agents. Overall, the research on CaN recombinant proteins is vital for advancing our comprehension of calcium-dependent signaling and its implications in health and disease.
