Analytical Data
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Gene name
Biotinidase/BTD
- Application
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Alternative Names
(Biotinase)
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Species
Human
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Source
E. coli
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Tag
N- His-GST & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P43251
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Expression Region
322-397aa
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Molecular Weight
41.3 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
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Protein Description
Biotinidase (BTD) is an essential enzyme responsible for recycling biotin, a crucial B-vitamin necessary for fatty acid synthesis, amino acid metabolism, and glucose homeostasis. Deficiency in biotinidase can lead to biotinidase deficiency disorder, a genetic condition that can result in neurological impairment, skin rashes, and immune dysfunction if left untreated. Research on recombinant biotinidase has gained prominence due to the potential for therapeutic interventions and better understanding of its structure-function relationships. Recombinant technologies enable the production of the enzyme in sufficient quantities for detailed biochemical analysis, facilitating the investigation of its catalytic mechanisms and stability. Additionally, studying BTD in a recombinant context supports the development of enzyme replacement therapies, particularly for patients with inherited biotinidase deficiencies. There is a growing interest in elucidating the molecular basis of various mutations associated with BTD deficiency to aid in genetic counseling and early diagnosis. By exploring recombinant forms of the enzyme, scientists aim to uncover novel insights into its role in metabolic pathways and its potential as a therapeutic target, ultimately contributing to improved healthcare outcomes for affected individuals.
