Analytical Data
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Gene name
BCAT2
- Application
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Alternative Names
Placental protein 18 ;PP18
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15382
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Expression Region
28-392aa
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Molecular Weight
57.3 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
Related Products
Protein Description
BCAT2 (branched-chain amino acid transaminase 2) is an important enzyme that plays a crucial role in the metabolism of branched-chain amino acids (BCAAs) such as leucine, isoleucine, and valine. These amino acids are essential for numerous physiological functions, including protein synthesis, energy production, and the regulation of metabolic pathways. Research has shown that BCAT2 is predominantly expressed in the brain and skeletal muscle, suggesting its vital role in amino acid catabolism and neurotransmitter synthesis. Alterations in BCAT2 activity have been linked to various metabolic disorders, including obesity, diabetes, and neurological diseases. Given its significance, recombinant protein studies of BCAT2 have gained traction, allowing scientists to elucidate its enzymatic mechanisms, identify potential inhibitors, and explore its role in metabolic regulation. Utilizing recombinant DNA technology, researchers can produce BCAT2 in heterologous systems, facilitating detailed biochemical analyses and structural studies. This research is not only pivotal for understanding the enzyme's function but also for developing therapeutic strategies aimed at modulating BCAA metabolism in various health conditions. As a potential target for drug development, BCAT2 offers promising avenues for intervention in metabolic dysfunctions, making it a critical focus in metabolic and neurological research.
