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AB28082

FITC Anti-Glycophorin A antibody [YTH89.1]

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(3 Publications)

Rat Monoclonal Glycophorin A antibody - conjugated to FITC. Suitable for Flow Cyt and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human GYPA.

View Alternative Names

CD235a, GPA, MNS, GYPA, Glycophorin-A, MN sialoglycoprotein, PAS-2, Sialoglycoprotein alpha

1 Images
Flow Cytometry - FITC Anti-Glycophorin A antibody [YTH89.1] (AB28082)
  • Flow Cyt

Unknown

Flow Cytometry - FITC Anti-Glycophorin A antibody [YTH89.1] (AB28082)

Staining of human peripheral blood erythrocytes with neat rat anti human CD235a : FITC (ab28082)

Key facts

Host species

Rat

Clonality

Monoclonal

Clone number

YTH89.1

Isotype

IgG2b

Conjugation

FITC

Excitation/Emission

Ex: 495nm, Em: 519nm

Carrier free

No

Reacts with

Human

Applications

Flow Cyt

applications

Immunogen

Native Full Length Protein corresponding to Human GYPA.

P02724

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Precipitation Ammonium Sulphate
Purification notes
Ig fraction prepared by ammonium sulphate precipitation
Storage buffer
pH: 7.4 Preservative: 0.09% Sodium azide Constituents: PBS, 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Glycophorin A also known as CD235a is a major glycoprotein of red blood cell membranes with a mass around 31 kDa. It is importantly expressed on the surface of erythrocytes. Glycophorin A plays an important role in maintaining cell membrane integrity and is associated with various antigenic sites which are important for compatibility testing. Researchers often detect Glycophorin A using antibodies such as Glycophorin A APC or Glycophorin A FITC in flow cytometry studies due to its distinct expression on red blood cells.
Biological function summary

Glycophorin A interacts with other membrane proteins to form part of the membrane's skeletal protein network. This network stabilizes the erythrocyte structure and contributes to its flexibility essential for passing through narrow capillaries. Glycophorin A does not form part of any large multiprotein complex but does interact with other glycophorins such as Glycophorin B. These interactions help to form the MN and Ss blood group antigens.

Pathways

Glycophorin A is involved in several pathways including the erythrocyte development and lipid raft pathways. These pathways are important for cell signaling and membrane transport processes. Glycophorin A's role in erythrocyte development is connected to protein 4.1R which links the membrane to the underlying cytoskeleton influencing red blood cell shape and stability. Additionally its role in lipid raft-mediated signaling intersects with proteins involved in immune response regulation.

Glycophorin A has associations with several conditions including malaria and hereditary spherocytosis. The interaction between Plasmodium falciparum and Glycophorin A contributes to the parasite's ability to invade erythrocytes indicating its relevance in malaria research. Additionally abnormalities with Glycophorin A expression or structure can lead to hereditary spherocytosis often related to a disruption in its interaction with ankyrin another structural protein. Understanding these associations helps elucidate the pathological mechanisms and potential therapeutic targets for these diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed : 35835865). 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.. (Microbial infection) Appears to be a receptor for Hepatitis A virus (HAV).. (Microbial infection) Receptor for P.falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans.
See full target information GYPA

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada 24:713-728 PubMed30588913

2018

The Impact of Two Combined Oral Contraceptives Containing Ethinyl Estradiol and Drospirenone on Whole Blood Clot Viscoelasticity and the Biophysical and Biochemical Characteristics of Erythrocytes.

Applications

Unspecified application

Species

Unspecified reactive species

Odette Emmerson,Janette Bester,Barend G Lindeque,Albe C Swanepoel

Antimicrobial agents and chemotherapy 58:4737-44 PubMed24913163

2014

Scalable preparation and differential pharmacologic and toxicologic profiles of primaquine enantiomers.

Applications

Flow Cyt

Species

Mouse

N P Dhammika Nanayakkara,Babu L Tekwani,H M T Bandara Herath,Rajnish Sahu,Montip Gettayacamin,Anchalee Tungtaeng,Yvonne van Gessel,Paul Baresel,Kristina S Wickham,Marilyn S Bartlett,Frank R Fronczek,Victor Melendez,Colin Ohrt,Gregory A Reichard,James D McChesney,Rosemary Rochford,Larry A Walker

Journal of immunology (Baltimore, Md. : 1950) 151:2124-31 PubMed7688394

1993

Biotinylation of monoclonal antibodies prevents their ability to activate the classical pathway of complement.

Applications

Unspecified application

Species

Unspecified reactive species

T S Jokiranta,S Meri
View all publications

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