Analytical Data
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基因名
GAL2
- Application
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别名
GAL2;GALNR2;Galanin receptor type 2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P05162
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表达区间
1-132aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMTGELEVKNMDMKPGSTLKITGSIADGTDG FVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGS EVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKL KE
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分子量
17 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












