Analytical Data
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Gene name
CIT
- Application
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Alternative Names
CIT; citron (rho-interacting, serine/threonine kinase 21); citron Rho-interacting kinase; CRIK; KIAA0949; STK21; serine/threonine-protein kinase 21
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O14578-1
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Expression Region
M1-Q499
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Protein Length
Partial
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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
CIT (Citrate Synthase) is an essential enzyme in the citric acid cycle, pivotal for cellular respiration and metabolic processes. Research into CIT recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. As the understanding of metabolic pathways expands, the need for producing large quantities of functional CIT for biochemical studies and therapeutic uses has intensified. Utilizing recombinant DNA technology, scientists can express CIT in host organisms, such as bacteria or yeast, enabling the purification of high-quality proteins for further investigation. This approach not only facilitates the study of the enzyme's structure and function but also aids in the exploration of its role in various diseases, including metabolic disorders and cancer. Additionally, CIT recombinant proteins can serve as valuable tools in developing novel diagnostic methods and therapeutic strategies. Given the escalating interest in metabolic engineering and synthetic biology, the production and characterization of CIT recombinant proteins hold promise for advancing both fundamental biology and practical applications in health and industry.
