Analytical Data
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Gene name
CKMT1A
- Application
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Alternative Names
CKMT; CKMT1-A; Mia-CK; U-MtCK; Creatine kinase U-type, mitochondrial; Ubiquitous mitochondrial creatine kinase; Acidic-type mitochondrial creatine kinase
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Species
Mouse
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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
P30275
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Expression Region
Glu43~Ile251
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Molecular Weight
28kDa
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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
CKMT1A, or creatine kinase, mitochondrial 1A, is a crucial enzyme involved in energy metabolism, particularly in the regulation of ATP levels within mitochondria. This enzyme is primarily expressed in the heart and skeletal muscles, where it plays a significant role in maintaining cellular energy homeostasis. Mutations in the CKMT1A gene have been linked to various neuromuscular disorders, revealing its critical importance in muscle function and overall energy balance. The study of CKMT1A recombinant protein allows researchers to better understand its structural and functional properties, as well as its role in pathophysiological conditions. By elucidating the enzymatic mechanisms and interactions of CKMT1A, researchers aim to uncover potential therapeutic targets for diseases associated with energy deficiency, such as mitochondrial myopathies. Furthermore, the recombinant form of CKMT1A can be utilized in various biochemical assays, aiding in the development of drugs that can modulate its activity. Overall, research on CKMT1A not only enhances our understanding of mitochondrial function but also holds promise for advancing treatment strategies for energy-related disorders.
