Analytical Data
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Gene name
Calumenin
- Application
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Alternative Names
Crocalbin
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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 95% as determined by SDS-PAGE.
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Uniprot
O43852
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Expression Region
Lys20~Phe315
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Molecular Weight
49kDa
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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
Calumenin is a calcium-binding protein belonging to the EF-hand family, which has garnered interest due to its potential roles in various cellular processes, including calcium signaling, protein folding, and stress responses in the endoplasmic reticulum (ER). Research into Calumenin has been propelled by the understanding that calcium homeostasis is critical for numerous physiological functions, and dysregulation can lead to various diseases, including neurodegenerative disorders and cancers. The emphasis on recombinant Calumenin synthesis has emerged as researchers aim to elucidate its structure-function relationship and cellular mechanisms. By producing Calumenin as a recombinant protein, scientists can investigate its binding properties, interaction with other proteins, and effects on calcium modulation under controlled conditions. This study further extends to exploring how Calumenin impacts cellular stress responses and the overall stability of proteins within the ER, which are crucial for maintaining cellular health. Additionally, recombinant Calumenin can serve as a valuable tool for therapeutic applications, including the development of strategies to mitigate calcium-related disorders. Overall, the research into recombinant Calumenin is pivotal for advancing our understanding of calcium-binding proteins and their implications in both fundamental biology and disease pathogenesis.
