Analytical Data
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Gene name
CALML3
- Application
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Alternative Names
CaM-like protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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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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Molecular Weight
43.9 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
CALML3 (Calmodulin-Like Protein 3) is a member of the calmodulin superfamily, known for its role in calcium signaling and various cellular processes. Research into CALML3 has gained traction due to its potential implications in health and disease, particularly in cancer biology, neurodegenerative disorders, and heart diseases. CALML3 has been implicated in the regulation of calcium-dependent signaling pathways, influencing processes such as cell proliferation, apoptosis, and differentiation. Its ability to bind calcium ions and interact with various target proteins underscores its importance in modulating cellular functions. Additionally, abnormalities in CALML3 expression or function have been associated with pathological conditions, prompting investigations into its role as a therapeutic target or biomarker. Given the complexity of calcium signaling networks, studying CALML3 protein expression, structure, and interactions can provide insights into its physiological roles and therapeutic potential. Advances in protein engineering and recombinant DNA technology have facilitated the production of CALML3 for detailed structural and functional studies, which are essential for understanding how it contributes to health and disease. These insights could pave the way for novel treatment strategies that harness the regulatory mechanisms governed by CALML3, highlighting the importance of continued research in this area. Thus, the study of CALML3 not only enriches our understanding of calcium signaling but also opens avenues for innovative therapeutic interventions.
