Analytical Data
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基因名
STT3B
- Application
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别名
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B; Homolog of yeast STT3; Oligosaccharyl transferase subunit STT3B; SIMP; source of immunodominant MHC associated peptides; Source of immunodominant MHC-associated peptides homolog; STT3 subunit of the oligosaccharyltransferase complex homolog B (S. cerevisiae); STT3 subunit of the oligosaccharyltransferase complex homolog B; STT3-B; Stt3b; STT3B_HUMAN
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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
Q8TCJ2
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表达区间
1-225 aa
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氨基酸序列
MSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRTLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKIFKKTV
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分子量
52.7 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
STT3B is a key component of the oligosaccharyltransferase (OST) complex, responsible for the N-glycosylation of proteins in the endoplasmic reticulum. N-glycosylation is a critical post-translational modification that influences protein folding, stability, and function. Mutations or dysfunction in STT3B can lead to various congenital disorders of glycosylation, resulting in significant clinical manifestations. Recent advances in structural biology and biochemistry have provided insights into the dynamic mechanisms of STT3B during protein glycosylation. Understanding the role of STT3B in glycosylation pathways is essential, as it holds potential therapeutic implications for treating diseases associated with glycosylation defects. Researchers are actively exploring the biochemical properties of STT3B and its interactions within the OST complex, aiming to elucidate the precise steps of glycosylation. This research not only sheds light on fundamental biological processes but also opens avenues for the development of treatments designed to address the consequences of improper glycosylation, potentially improving patient outcomes in related disorders.
