Analytical Data
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Gene name
ILVBL
- Application
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Alternative Names
IlvB-like protein
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Species
Human
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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
A1L0T0
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Expression Region
1-632aa
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Molecular Weight
70.7 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
ILVBL (isovaleryl-CoA dehydrogenase-like protein) is a member of the acyl-CoA dehydrogenase family, which plays a crucial role in the mitochondrial fatty acid oxidation and branched-chain amino acid metabolism. The importance of ILVBL arises from its involvement in various metabolic pathways essential for energy production and metabolic homeostasis. Mutations or dysfunction in ILVBL have been linked to metabolic disorders, which can result in significant health issues, including energy metabolism impairments and neurological symptoms. Understanding the structure and function of ILVBL is vital for elucidating its role in these metabolic pathways and may lead to potential therapeutic targets for conditions associated with its dysregulation. Recent advances in recombinant technology have enabled the expression and purification of ILVBL protein, facilitating in-depth biochemical and structural studies. These investigations aim to shed light on its enzymatic mechanisms and regulation, paving the way for novel insights into metabolic diseases and potential interventions. By exploring the functional dynamics of ILVBL, researchers hope to contribute to the understanding of metabolic pathways and develop strategies to counteract the effects of metabolic disorders.
