Analytical Data
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基因名
ALG9
- Application
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别名
ALG9; ALG9_HUMAN; Alpha-1.2-mannosyltransferase ALG9
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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
Q9H6U8
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表达区间
1-618aa
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氨基酸序列
MASRGARQRLKGSGASSGDTAPAADKLRELLGSREAGGAEHRTELSGNKAGQVWAPEGSTAFKCLLSARLCAALLSNISDCDETFNYWEPTHYLIYGEGFQTWEYSPAYAIRSYAYLLLHAWPAAFHARILQTNKILVFYFLRCLLAFVSCICELYFYKAVCKKFGLHVSRMMLAFLVLSTGMFCSSSAFLPSSFCMYTTLIAMTGWYMDKTSIAVLGVAAGAILGWPFSAALGLPIAFDLLVMKHRWKSFFHWSLMALILFLVPVVVIDSYYYGKLVIAPLNIVLYNIFTPHGPDLYGTEPWYFYLINGFLNFNVAFALALLVLPLTSLMEYLLQRFHVQNLGHPYWLTLAPMYIWFIIFFIQPHKEERFLFPVYPLICLCGAVALSALQHSFLYFQKCYHFVFQRYRLEHYTVTSNWLALGTVFLFGLLSFSRSVALFRGYHGPLDLYPEFYRIATDPTIHTVPEGRPVNVCVGKEWYRFPSSFLLPDNWQLQFIPSEFRGQLPKPFAEGPLATRIVPTDMNDQNLEEPSRYIDISKCHYLVDLDTMRETPREPKYSSNKEEWISLAYRPFLDASRSSKLLRAFYVPFLSDQYTVYVNYTILKPRKAKQIRKKSGG
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分子量
97.2 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
ALG9 is a crucial enzyme involved in the oligosaccharide synthesis pathway within the endoplasmic reticulum, specifically playing a significant role in the early stages of N-linked glycosylation. This process is vital for protein folding, stability, and function, with implications across various biological systems. Mutations and dysregulations in the ALG9 gene have been linked to several congenital disorders of glycosylation (CDGs), demonstrating its importance in human health. Research into ALG9 recombinant protein has gained momentum due to its potential applications in understanding glycosylation-related diseases and developing novel therapeutic strategies. By producing and characterizing ALG9 in vitro, scientists aim to elucidate its function, define its substrate specificities, and explore its interaction with other glycosylation enzymes. Furthermore, insights gained from ALG9 studies could contribute to the development of diagnostic tools and therapeutic interventions for CDGs and other glycosylation disorders, making ALG9 a focal point in the field of glycobiology and biomedicine. The exploration of ALG9 also holds promise for advancing biotechnological applications, particularly in the production of glycosylated therapeutic proteins with enhanced efficacy and safety profiles. Overall, the ongoing research into ALG9 recombinant protein serves both fundamental scientific inquiries and practical clinical needs, highlighting its significance in the study of glycosylation and its broader implications for human health.
