Analytical Data
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Gene name
GYPB
- Application
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Alternative Names
PAS-3 SS-active sialoglycoprotein Sialoglycoprotein delta CD_antigen: CD235b
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Species
Human
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Source
E. coli
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Tag
N- His
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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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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
Related Products
Protein Description
GYPB, or Glycophorin B, is a sialoglycoprotein primarily expressed on the surface of red blood cells, playing a critical role in maintaining erythrocyte membrane stability and influencing blood group antigenicity. Research into GYPB and its recombinant forms has gained traction due to its potential applications in transfusion medicine and its relevance in studying hemolytic diseases and other hematological disorders. The reconstitution of GYPB in vitro allows for a detailed understanding of its structural and functional properties, as well as its interactions with other blood cell components. Furthermore, advances in genetic engineering and protein expression systems have enabled scientists to produce recombinant GYPB proteins, facilitating the exploration of antibody responses and the development of diagnostic tools. Understanding the molecular mechanisms by which GYPB operates is essential for elucidating its role in cell signaling and immune responses, ultimately enhancing our knowledge of red blood cell physiology and pathology. The ongoing investigations into GYPB serve not only to illuminate the complexities of red blood cell biology but also to pave the way for novel therapeutic strategies targeting various blood-related conditions.
