Analytical Data
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Gene name
CALML3
- Application
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Alternative Names
CALML3；Calmodulin-like Protein 3
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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
P27482
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Expression Region
1-149aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMADQLTEEQVTEFKEAFSLFDKDGDG CITTRELGTVMRSLGQNPTEAELRDMMSEIDRDGNGTVDFPEFLGMMARK MKDTDNEEEIREAFRVFDKDGNGFVSAAELRHVMTRLGEKLSDEEVDEMI RAADTDGDGQVNYEEFVRVLVSK
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Molecular Weight
19 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
CALML3, a member of the calmodulin-like protein family, plays a crucial role in various cellular processes by acting as a calcium sensor and modulator. Its expression is primarily observed in the brain and other tissues, indicating its potential involvement in neuronal signaling and other physiological functions. Recent studies have suggested that CALML3 may be implicated in several pathological conditions, including cancer and neurodegenerative diseases, making it a target of interest for therapeutic intervention. The ability of CALML3 to interact with multiple proteins and influence calcium-dependent signaling pathways highlights its significance in maintaining cellular homeostasis. However, the molecular mechanisms underlying CALML3's function remain poorly understood, necessitating further research. Since recombinant proteins provide a valuable tool for elucidating the structure-function relationship of proteins, researchers are increasingly focused on the expression and characterization of CALML3 as a recombinant protein. Such studies aim to unravel its biological roles and potential interactions with other cellular components, paving the way for new strategies in drug development and disease management. Through the systematic study of CALML3, including its binding affinities, structural dynamics, and cellular interactions, scientists seek to gain insights that could ultimately lead to novel therapeutic approaches targeting calcium signaling pathways in various diseases.
