Analytical Data
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Gene name
GYPE
- Application
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Alternative Names
GYP-E; MNS; GPE; MiIX
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15421
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Expression Region
Ser20~Ile70
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Molecular Weight
38kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
