Analytical Data
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基因名
GGN
- Application
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别名
FLJ35713; Gametogenetin; Ggn; GGN_HUMAN; MGC33369
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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
Q86UU5
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表达区间
1-652aa
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氨基酸序列
MGNLQSEPSAGGGSRKVQPSDRAPDSRRTSLVEPEMTSQAMRLTRGLGVWFPGSATPPGLMVPREPQASPSTLPLTLERPSPVMPPPEEAAAVSAPPPAPAGTLLPGPSKWQKPAGTPVPRIRRLLEASHRGQGDPPSLRPLKPPPPPRQLSVKDTVPRAPSQFPPPLETWKPPPPLPSERQPADRRITPALATPASPPTESQAGPRNQGQTAGRARGGAPPHAGEGEMAQPADSESGLSLLCKITFKSRPSLAPPAASSSLAAKASLGGGGGGGLFAASGAISYAEVLKQGPLPPGAARPLGEVSRGAQEAEGGDGDGEGCSGPPSAPASQARALPPPPYTTFPGSKPKFDWVSAPDGPERHFRFNGAGGGIGAPRRRAAALSGPWGSPPPPPEQIHSAPGPRRPAPALLAPPTFIFPAPTNGEPMRPGPPGLQELPPLPPPTPPPTLQPPALQPTPLPVAPPLTPGLGHKESALAPTAAPALPPALAADQAPAPSPAPAPTVAEPSPPVSAPAPAAAPIKTRTRRNKGSRAARGATRKDGLHGDGPRERATATVPDSSGGGGGGSGASQTGAANTRAARHWLPFQVLNSCPCKCYCHHQPRHRRLPRNVSAWLSTSTNHLGEPPWVATIKLSGSLVAKLEHYDLQATHSN
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分子量
93.1 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
GGN (Glycogenin) is a crucial protein involved in the initiation of glycogen synthesis, serving as a primer for glycogen synthase in the formation of glucose polymer chains. Understanding the structure and function of GGN is essential due to its critical role in regulating glucose metabolism and maintaining energy homeostasis in various tissues. Dysregulation of glycogen metabolism can lead to metabolic disorders, including diabetes and glycogen storage diseases. Recent studies have highlighted the potential of GGN as a therapeutic target for these conditions, prompting further investigation into its molecular mechanisms and interactions with other metabolic pathways. Advances in recombinant protein technology have enabled researchers to produce GGN in vitro, facilitating detailed studies of its biochemical properties and functions. By employing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR), scientists aim to elucidate the three-dimensional structure of GGN and identify key sites for enzymatic activity. Furthermore, the development of GGN-based assays holds promise for screening potential drug candidates that can modulate its activity, offering new avenues for therapeutic intervention in metabolic diseases. The ongoing research into GGN and its role in glycogen metabolism not only enhances our understanding of fundamental biological processes but also paves the way for innovative approaches to tackle associated health issues, thus underscoring its significance in both basic and applied biomedical research.
