G5017
Glycophorin Predominantly glycophorin A from blood type MN
lyophilized powder
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About This Item
biological source
human blood (type MN)
Quality Level
form
lyophilized powder
solubility
soluble 1.00-1.10 mg/mL
H2O: soluble, clear to hazy
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... GYPA(2993)
Related Categories
General description
Glycophorin (GYPA), a sialoglycoprotein, is present in human erythrocytes that carry antigens M and N of the MN blood group. The GYPA gene is mapped to human chromosome 4q31.21.
Glycophorin A cconsists of a glycosylated extracellular domain, a single transmembrane α-helix and a cytoplasmic COOH-terminal domain.
Application
Glycophorin A (GpA) is used as a model system for extensive experimental, theoretical, and simulation studies focusing on TM protein association. Glycophorin A is used to study the mechanism of kinase activation in the receptor for colony-stimulating factor 1. It is used to analyse glycoproteins separated by two-dimensional gel electrophoresis.
Glycophorin Predominantly glycophorin A from blood type MN has been used:
- as a standard in Amide-80 column size-based separation for the characterization of plasma-type O-linked sugar chains
- to screen the P. falciparum phage library using biopanning method,
- as a phosphocholine-free component to test its reactivity with antibodies over a saccharide-bound enzyme-linked immunosorbent assay (ELISA)
Biochem/physiol Actions
Glycophorin (GYPA) is involved in the mode of entry of the Plasmodium falciparum parasite into erythrocytes. It is also implicated in intraplaque hemorrhage as well as in the macrophage infiltration in coronary atheromas.
A membrane glycoprotein with several isoforms that interact with other membrane proteins to confer shape and antigenicity to erythrocytes.
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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S Raffy et al.
The Journal of biological chemistry, 272(41), 25524-25530 (1997-11-05)
Previously we demonstrated that transmembrane back insertion of glycophorin A, a solubilizable intrinsic protein, can be obtained in dipalmitoylphosphatidylcholine multilamellar vesicles, MLVs, by electropulsation (Raffy, S., and Teissié, J. (1995) Eur. J. Biochem. 230, 722-732). Here we report that transmembrane
C J Pan
Zhonghua bing li xue za zhi = Chinese journal of pathology, 21(4), 224-226 (1992-08-01)
Eighteen cases of anaplastic meningioma were studied by LM, EM and immunohistochemistry for vimentin, EMA, keratin, GFAP and S-100. Microscopically, there were four histologic types, i.e. fibrosarcoma-like, angiosarcoma-like, polymorphic giant cell sarcoma-like and angiopapillary structure. By EM, four kinds of
Xuerong Li et al.
Molecular and biochemical parasitology, 183(1), 23-31 (2012-01-26)
The malaria parasite Plasmodium falciparum invades human erythrocytes through multiple pathways utilizing several ligand-receptor interactions. These interactions are broadly classified in two groups according to their dependency on sialic acid residues. Here, we focus on the sialic acid-dependent pathway by
A W Lee et al.
Proceedings of the National Academy of Sciences of the United States of America, 87(18), 7270-7274 (1990-09-01)
Receptor tyrosine kinases remain dormant until activated by ligand binding to the extracellular domain. Two mechanisms have been proposed for kinase activation: (i) ligand binding to the external domain of a receptor monomer may induce a conformational change that is
Possible exacerbation of myasthenia gravis by ciprofloxacin.
B Moore et al.
Lancet (London, England), 1(8590), 882-882 (1988-04-16)
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