Analytical Data
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基因名
Eogt
- Application
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别名
Eogt；AER61；C3orf64；EOGT1;EGF domain-specific O-linked N-acetylglucosamine transferase
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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
Q5NDL2
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表达区间
18-527aa
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氨基酸序列
GQN EAPPNTHSIP GEPLYNYASI RLPEEHIPFF LHNNRHIATV CRKDSLCPYK KHLEKLKYCW GYEKSCKPEF RFGYPVCSYV DMGWTDTLES AEDIFWKQAD FGYARERLEE MHVLCQPKET SDSSLVCSRY LQYCRATNLY LDLRNIKRNH DRFKEDFFQS GEIGGHCKLD IRTLTSEGQR KSPLQSWFAE LQSYTQLNFR PIEDAKCDIV IEKPTYFMKL DAGVNMYHHF CDFINLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW NAFTDYDVIH LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFAQHVL HRLNITQEGP KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV DYKYRELGFL DQLRITHNTD IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKHDEL
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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
Eogt, or EGF-like domain-containing protein O-glycosyltransferase, is a critical enzyme involved in the modification of proteins via O-glycosylation, a post-translational modification that adds sugar moieties to serine and threonine residues. This process is essential for the proper functioning of various proteins, influencing their stability, localization, and activity. Research into Eogt has gained prominence due to its potential implications in human health and disease, particularly in cancer, where aberrant glycosylation patterns are often observed. The study of Eogt not only enhances our understanding of O-glycosylation mechanisms but also presents opportunities for therapeutic interventions. By elucidating the structural and functional characteristics of Eogt, researchers aim to uncover its role in cellular processes and pathology. Furthermore, the development of Eogt inhibitors could offer novel strategies for targeting tumor growth and progression, making it a promising subject of study in the field of glycobiology and cancer research. As a result, ongoing investigations into Eogt's enzymatic function and regulatory mechanisms are critical for advancing our knowledge on glycosylation and its implications in health and disease.
