Mouse Monoclonal Glycophorin A antibody - conjugated to FITC. Suitable for Flow Cyt and reacts with Human samples. Immunogen corresponding to Synthetic Peptide within Human GYPA.
IgG2b
Mouse
FITC
Ex: 495nm, Em: 519nm
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: PBS, 0.2% BSA
Liquid
Monoclonal
Flow Cyt | |
---|---|
Human | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info - | Notes 20 μl reagent / 100 μl of whole blood or 106 cells in a suspension. |
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Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).
Glycophorin-A, MN sialoglycoprotein, PAS-2, Sialoglycoprotein alpha, GPA, GYPA
Mouse Monoclonal Glycophorin A antibody - conjugated to FITC. Suitable for Flow Cyt and reacts with Human samples. Immunogen corresponding to Synthetic Peptide within Human GYPA.
Glycophorin-A, MN sialoglycoprotein, PAS-2, Sialoglycoprotein alpha, GPA, GYPA
IgG2b
Mouse
FITC
Ex: 495nm, Em: 519nm
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: PBS, 0.2% BSA
Liquid
Monoclonal
HIR2
Affinity purification Protein G
ab52452 recognises N-terminal, homologous portion of glycophorins A (GPA) and B (GPB) which are single-pass membrane sialoglycoproteins expressed on red blood cells and erythroid precursor cells.
Prior to conjugation, ab52452 was purified by Protein G affinity chromatography. After conjugation, it was purified by site exclusion chromatography. Purity >95% by SDS-PAGE.
Blue Ice
+4°C
ab52452 agglutinates untreated RBCs but it failes to agglutinate papain-treated cells, binds to GPA, but weakly to GPB. The antibody is useful in erythroid cell development studies, because HIR2 antigen is expressed on early erythroblasts, late erythroblasts, erythroblasts, mature erythrocytes and the cells of erythroid cell lines K562 and HEL, but not on all other cells (mature erythrocytes are characteristically CD235a positive and CD45 and CD71 negative).
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Glycophorin A and Glycophorin B are well-known sialoglycoproteins located on the surface of human erythrocytes. They are often referenced by alternate names like GYPHE for Glycophorin E and Glycophorin A+B for the combination of both proteins. Glycophorin A which can be labeled with FITC for detection has a molecular mass of approximately 31.3 kDa while Glycophorin B has a similar but slightly smaller mass. These proteins are essential components of the erythrocyte membrane contributing significantly to the negative charge and structural stability of red blood cells.
Glycophorins A and B interact with other proteins in the erythrocyte membrane influencing the cell's architecture and the stability of the cytoskeleton. These glycophorins associate with CD235a known for its role in red blood cell recognition and interactions. Glycophorin A participates in the formation of a protein complex with other membrane proteins contributing to the antigenic properties of red blood cells which is important in blood transfusion biology.
Glycophorin A and B participate in several key biological processes such as membrane organization and signal transduction pathways. They are involved in the MNS blood group system and interact with proteins like band 3 which is a critical component of the erythrocyte's anion exchange mechanism. This interaction helps facilitate ion transport and gas exchange in red blood cells.
Glycophorins A and B have associations with malaria and autoimmune hemolytic anemia. The malaria parasite Plasmodium falciparum interacts with these glycophorins to invade red blood cells. Changes in the glycan composition of glycophorin A contribute to the pathophysiology of certain autoimmune disorders potentially linking to immune recognition proteins. Managing these interactions and modifications can be important in designing therapeutic interventions for these conditions.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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Flow cytometry analysis (surface staining) of human peripheral blood labeling CD235a with ab52452.
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