Analytical Data
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Gene name
Calmodulin
- Application
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Alternative Names
CALM1; CALM; CAM; CAM1Calmodulin-1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DP23
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Expression Region
2-149aa
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Molecular Weight
32.7 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
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Protein Description
Calmodulin (CaM) is a highly conserved calcium-binding messenger protein found in all eukaryotic cells, playing a crucial role in various cellular processes by modulating the activity of numerous target proteins in response to fluctuations in intracellular calcium levels. Its ability to bind calcium ions induces conformational changes that enable it to interact with a wide range of proteins, including kinases, phosphatases, and ion channels, thus influencing pathways such as muscle contraction, cell division, and neurotransmission. The recombinant expression of calmodulin in various systems, such as Escherichia coli or yeast, has facilitated the study of its structural and functional properties, allowing researchers to investigate its interactions with target proteins and its role in signaling pathways. Understanding calmodulin's mechanisms can provide valuable insights into cellular functions and disease states, including cardiac disorders and neurodegenerative diseases, where calcium signaling is often disrupted. Moreover, the study of calmodulin's interactions has implications for drug discovery, as targeting calmodulin-related pathways may yield novel therapeutic strategies. With advances in protein engineering and expression technologies, researchers continue to explore the versatility of recombinant calmodulin for applications in biochemistry, pharmacology, and synthetic biology, paving the way for innovative solutions in biomedical research.
