Analytical Data
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Gene name
GAL2
- Application
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Alternative Names
GAL2；GALNR2；Galanin receptor type 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05162
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Expression Region
1-132aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTGELEVKNMDMKPGSTLKITGSIADGTDG FVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGS EVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKL KE
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Molecular Weight
17 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
GAL2, or galactose-1-phosphate uridylyltransferase, is an essential enzyme in the galactose metabolism pathway, primarily involved in the conversion of galactose to glucose, a crucial process for energy production in organisms. Its dysfunction can lead to galactosemia, a genetic disorder characterized by an inability to metabolize galactose, resulting in severe health issues, including liver damage, developmental delays, and cognitive impairments. Studies have shown that the GAL2 protein exhibits distinct structural and functional properties that are critical for its enzymatic activity. Understanding these properties can provide insight into the molecular mechanisms underlying galactose metabolism and the pathophysiology of related disorders. Furthermore, the recombinant expression and purification of GAL2 can facilitate kinetic and structural studies, potentially leading to therapeutic advancements. Research on GAL2 not only contributes to the broader field of metabolic enzyme studies but also offers possibilities for designing targeted interventions and improving management strategies for individuals affected by galactosemia. In this context, characterizing GAL2 through recombinant protein techniques is crucial for elucidating its functional roles, enhancing our understanding of its interaction with other metabolic pathways, and paving the way for innovative approaches in clinical settings.
