Analytical Data
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Gene name
Bmal1
- Application
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Alternative Names
Arnt3 (Brain and muscle ARNT-like 1) (Bmal1)
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Species
Mouse
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Source
E. coli
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Tag
C- His-Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9WTL8
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Expression Region
49-434aa
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Molecular Weight
46.5 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
The study of Bmal1 recombinant protein is rooted in its pivotal role in the regulation of circadian rhythms, which are essential for maintaining various physiological processes in living organisms. Bmal1, or Brain and Muscle Arnt-Like 1, is a core component of the molecular clock, functioning as a transcription factor that, in combination with Clock, activates the expression of other circadian genes. Understanding its structure and function is crucial, as disruptions in circadian rhythms have been associated with numerous health issues, including metabolic disorders, sleep disturbances, and certain types of cancer. Researchers have sought to produce Bmal1 as a recombinant protein to investigate its biochemical properties, interactions with partner proteins, and regulatory mechanisms. Expressing Bmal1 in a controlled laboratory setting allows for detailed studies of its functional dynamics, including post-translational modifications and its role in circadian signaling pathways. Furthermore, by utilizing advanced techniques such as protein crystallography and molecular dynamics simulations, scientists aim to decipher the intricacies of Bmal1’s structure-function relationships. This knowledge could contribute to the development of novel therapeutic strategies targeting circadian misalignments, highlighting the importance of Bmal1 and its recombinant form in both basic and applied biological research.
