Analytical Data
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Gene name
GYPB
- Application
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Alternative Names
GYPB；GPB；Glycophorin-B
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P06028
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Expression Region
20-91aa
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AA Sequence
LSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAPVVIILIILCVMAGIIGTILLISYSIRRLIKA
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Molecular Weight
10.5 kDa
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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
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Protein Description
GYPB, or Glycophorin B, is a significant sialoglycoprotein primarily expressed on the surface of red blood cells, playing a crucial role in cell-cell interactions and imparting negative charge to the erythrocyte membrane, which influences blood circulation and immune evasion. The study of GYPB has gained attention due to its involvement in various hematological conditions, including transfusion reactions and certain blood disorders. Understanding its structure and function is vital for developing therapeutic interventions and improving blood transfusion compatibility. The exploration of GYPB as a recombinant protein has facilitated investigations into its biological properties and potential applications, such as in vaccine development and targeted therapies for conditions like malaria, where red blood cell interactions are pivotal. Research initiatives have focused on the expression, purification, and functional analysis of GYPB to unravel its molecular mechanisms and enhance its utility in clinical settings. Additionally, advancements in genetic engineering techniques have allowed for the precise modification of GYPB, leading to exciting prospects in biomedical research and therapeutic applications. As scientists continue to delve into the complexities of GYPB, its potential as a biomarker and therapeutic target in immunology and hematology remains a promising area of investigation, paving the way for innovative approaches to manage and treat blood-related diseases.
