Analytical Data
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Gene name
HADHB
- Application
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Alternative Names
TP-beta （Acetyl-CoA acyltransferase）（Beta-ketothiolase）
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99JY0
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Expression Region
35-475aa
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Molecular Weight
54.6 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
HADHB, or Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase multienzyme complex, plays a critical role in fatty acid catabolism and mitochondrial energy production. Mutations in the HADHB gene can lead to a rare metabolic disorder known as mitochondrial acyl-CoA dehydrogenase deficiency, associated with severe clinical manifestations, including hypoglycemia, cardiomyopathy, and neurological impairments. Research into HADHB recombinant proteins has become increasingly important as scientists aim to understand the enzyme's structure-function relationship and its regulation within metabolic pathways. Producing recombinant HADHB proteins allows for in-depth biochemical studies, such as enzyme kinetics, substrate specificity, and interaction with other metabolic enzymes. Additionally, these studies may provide insights into the molecular mechanisms underlying HADHB-related metabolic disorders, paving the way for potential therapeutic strategies. As the prevalence of metabolic diseases continues to rise globally, understanding the intricacies of HADHB enforces the relevance of this research in developing effective diagnostics and treatments, thereby improving patient care in affected individuals.
