Analytical Data
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Gene name
GYPA
- Application
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Alternative Names
GYPA；GPA；Glycophorin-A
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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
P02724
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Expression Region
1-150aa
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AA Sequence
MYGKIIFVLL LSAIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK SPSDVKPLPS PDTDVPLSSV EIENPETSDQ
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Molecular Weight
43 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
Glycophorin A (GYPA) is a significant sialoglycoprotein predominantly found on the surface of red blood cells, playing a crucial role in defining the ABO blood group and influencing various biological processes such as cell-cell interactions and immune responses. Research on GYPA has gained momentum due to its potential applications in transfusion medicine, understanding blood group antigens, and developing targeted therapies for blood-related disorders. The importance of GYPA extends beyond hematology; its structural properties and interactions with pathogens are of interest in virology and immunology, especially regarding how certain viruses exploit these glycoproteins for cell entry. The study of GYPA undergoes continuous evolution with advancements in recombinant protein technology, allowing for more detailed studies of its structure-function relationships. By utilizing recombinant GYPA, researchers can investigate the molecular mechanisms underlying blood group antigenicity and evaluate the potential for therapeutic applications, such as designing blood substitutes or developing vaccines against hemagglutinating viruses. The elucidation of GYPA's role in red blood cell physiology and pathophysiology highlights the need for comprehensive studies, driving research forward in both basic science and clinical applications.
