Analytical Data
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基因名
GYPE
- Application
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别名
GYP-E; MNS; GPE; MiIX
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种属
Human
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P15421
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表达区间
Ser20~Ile70
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分子量
38kDa
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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
GYPE, or Glycophorin E, is a member of the glycophorin family of transmembrane proteins primarily expressed in erythroid cells. Research on GYPE has gained traction due to its crucial role in facilitating cell-cell interactions and maintaining the integrity of red blood cells (RBCs). Understanding the restructuring or recombinant production of GYPE proteins is significant, as it offers insights into various hematological disorders and potential therapeutic avenues, such as blood transfusion compatibility and the development of artificial blood substitutes. The unique glycosylation patterns and structural properties of GYPE proteins make them compelling candidates for further study, particularly in the context of their functional roles in cell adhesion and signaling pathways. As researchers continue to explore GYPE's functional implications and develop recombinant forms for investigative purposes, there is a growing interest in the application of molecular biology techniques, such as gene cloning and expression systems, to produce GYPE at scale. This not only enhances the understanding of its biological function but also aims to address clinical needs related to transfusion medicine. The challenges in creating stable and biologically active recombinant GYPE underscore the importance of this research, paving the way for novel therapeutic strategies and diagnostic tools in the realm of blood-related health issues.












