Analytical Data
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基因名
GUP1
- Application
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别名
HHATL; C3orf3; GUP1; KIAA1173Protein-cysteine N-palmitoyltransferase HHAT-like protein; Glycerol uptake/transporter homolog; Hedgehog acyltransferase-like protein
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9HCP6
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表达区间
1-504aa
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氨基酸序列
MGIKTALPAAELGLYSLVLSGALAYAGRGLLEASQDGAHRKAFRESVRPGWEYIGRKMDVADFEWVMWFTSFRNVIIFALSGHVLFAKLCTMVAPKLRSWMYAVYGALAVMGTMGPWYLLLLLGHCVGLYVASLLGQPWLCLGLGLASLASFKMDPLISWQSGFVTGTFDLQEVLFHGGSSFTVLRCASFALESCAHPDRHYSLADLLKYNFYLPFFFFGPIMTFDRFHAQVSQVEPVRREGELWHIRAQAGLSVVAIMAVDIFFHFFYILTIPSDLKFANRLPDSALAGLAYSNLVYDWVKAAVLFGVVNTVACLDHLDPPQPPKCITALYVFTETHFDRGINDWLCKYVYNHIGGEHSAVIPELAATVATFAITTLWLGPCDIVYLWSFLNCFGLNFELWMQKLAEWGPLARIEASLSVQMSRRVRALFGAMNFWAIIMYNLVSLNSLKFTELVARRLLLTGFPQTTLSILFVTYCGVQLVKERERTLALEEEQKQDKEKPE
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分子量
83.1 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
GUP1 (Glycosylated/UDP-N-acetylglucosamine pyrophosphorylase 1) is a protein of considerable interest in molecular biology and biochemistry due to its role in glycoprotein synthesis and cellular signaling pathways. It is primarily involved in the metabolism of UDP-N-acetylglucosamine, a critical substrate for glycosylation processes. Understanding GUP1 is crucial not only for deciphering its functions in normal cellular physiology but also for exploring its implications in various diseases, including cancer and metabolic disorders. The study of GUP1 recombinant proteins is particularly significant as it allows researchers to dissect the structure-function relationships and post-translational modifications that influence its activity. By applying techniques such as recombinant DNA technology, scientists can produce GUP1 in heterologous systems like E. coli or yeast, facilitating the characterization of its enzymatic properties and interaction with other cellular components. Furthermore, the purified GUP1 protein can be utilized in high-throughput screening assays to identify potential inhibitors or modulators, paving the way for therapeutic interventions. Given its central role in glycosylation, elucidating the functional mechanisms of GUP1 may provide insight into developing novel strategies for disease treatment and understanding the complex regulatory networks that underpin cellular functions. Overall, the research on GUP1 recombinant protein stands at the intersection of fundamental science and potential clinical application, making it a topic of great relevance in contemporary biomedical research.
