Analytical Data
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基因名
ENAH
- Application
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别名
ENA; Enah; ENAH_HUMAN; MENA; NDPP1; Protein enabled homolog
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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
Q8N8S7
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表达区间
1-591aa
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氨基酸序列
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETGPTL PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER LERERMERER LERERLERER LERERLEQEQ LERERQERER QERLERQERL ERQERLERQE RLDRERQERQ ERERLERLER ERQERERQEQ LEREQLEWER ERRISSAAAP ASVETPLNSV LGDSSASEPG LQAASQPAET PSQQGIVLGP LAPPPPPPLP PGPAQASVAL PPPPGPPPPP PLPSTGPPPP PPPPPLPNQV PPPPPPPPAP PLPASGFFLA SMSEDNRPLT GLAAAIAGAK LRKVSRMEDT SFPSGGNAIG VNSASSKTDT GRGNGPLPLG GSGLMEEMSA LLARRRRIAE KGSTIETEQK EDKGEDSEPV TSKASSTSTP EPTRKPWERT NTMNGSKSPV ISRRDSPRKN QIVFDNRSYD SLHRPKSTPL SQPSANGVQT EGLDYDRLKQ DILDEMRKEL TKLKEELIDA IRQELSKSNT A
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分子量
66.5 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
ENDOGL1, a member of the endo-β-N-acetylglucosaminidase family, has garnered significant interest in the field of glycoscience and biomedical research due to its unique enzymatic properties and potential therapeutic applications. The enzyme is known for its ability to cleave N-linked glycans from glycoproteins, which plays a crucial role in modulating glycoprotein stability, activity, and clearance in biological systems. As glycosylation is a fundamental post-translational modification that influences protein folding, function, and immune responses, understanding the mechanisms of ENDOLG1 can provide insights into various physiological and pathological processes, including cancer progression, immune evasion, and viral infections. Recent studies have suggested that targeting ENDOLG1 may enhance the effectiveness of immunotherapies or serve as a novel approach to manipulating glycosylation patterns in therapeutic proteins, thereby improving their pharmacokinetics and therapeutic efficacy. Moreover, the recombinant production of ENDOLG1 allows for detailed biochemical characterization and the exploration of its functional role in various biological contexts, paving the way for its application in drug development and glycoprotein engineering. As such, the investigation of ENDOLG1 and its recombinant protein form is crucial for advancing our understanding of glycan biology and for exploring innovative strategies for therapeutic intervention in diseases associated with aberrant glycosylation.
