Analytical Data
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Gene name
HIBCH
- Application
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Alternative Names
Beta-Hydroxyisobutyryl-CoA Hydrolase
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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 90% as determined by SDS-PAGE.
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Uniprot
Q8QZS1
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Expression Region
Met1~Gly170
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Molecular Weight
22kDa
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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
HIBCH (3-hydroxyisobutyryl-CoA hydrolase) is an enzyme involved in the metabolism of branched-chain amino acids and plays a crucial role in the mitochondrial pathway of isobutyryl-CoA degradation. Mutations in the HIBCH gene have been linked to various metabolic disorders, particularly conditions affecting energy metabolism, leading to the accumulation of toxic metabolites. Given its essential function in cellular energy homeostasis, researchers have focused on elucidating the structure, function, and regulation of HIBCH to better understand its role in health and disease. Recent studies have employed recombinant DNA technology to produce HIBCH in a controlled laboratory environment, allowing for in-depth biochemical analyses and functional studies. The generation of recombinant HIBCH provides valuable insights into enzyme kinetics, substrate specificity, and potential therapeutic targets for metabolic disorders. Advancements in techniques such as X-ray crystallography and cryo-electron microscopy have further propelled research, enabling scientists to visualize the enzyme's structure and determine how mutations may disrupt its function. This comprehensive understanding of HIBCH not only aids in the diagnosis and treatment of metabolic diseases but also contributes to the broader field of metabolic research by highlighting the complexities of enzyme regulation and interaction within metabolic pathways.
