Analytical Data
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Gene name
CaN
- Application
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Alternative Names
CaN；PALBH；Calpain-7
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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
P00915
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Expression Region
2-261aa
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AA Sequence
ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF
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Molecular Weight
30.7 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 study of CaN (Calcineurin), a calcium/calmodulin-dependent serine/threonine phosphatase, has gained significant attention due to its crucial role in various cellular processes, particularly in the immune system and neuronal signaling. Calcineurin is activated by calcium-bound calmodulin, leading to a cascade of downstream signaling that regulates T-cell activation, cardiac function, and synaptic plasticity. Dysregulation of CaN has been implicated in a variety of diseases, including autoimmune disorders, heart failure, and neurodegenerative conditions. Given its pivotal function, recombinant CaN proteins are extensively studied for their biochemical properties and potential therapeutic applications. The production of these proteins in host systems like bacteria, yeast, or mammalian cells allows researchers to investigate their enzymatic activity, structural characteristics, and interactions with other signaling molecules. Furthermore, understanding the regulatory mechanisms of CaN can facilitate the design of specific inhibitors or enhancers that may serve as innovative treatments for diseases associated with its dysfunction. As such, the exploration of recombinant CaN proteins is instrumental in delineating the molecular underpinnings of calcium signaling and its implications for health and disease.
