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G5017

Sigma-Aldrich

Glycophorin Predominantly glycophorin A from blood type MN

lyophilized powder

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

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)

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Possible exacerbation of myasthenia gravis by ciprofloxacin.
B Moore et al.
Lancet (London, England), 1(8590), 882-882 (1988-04-16)
Hajime Mizukami et al.
Journal of human genetics, 50(12), 667-670 (2005-10-06)
Ten alleles (five M and five N alleles) of the MN blood group system with normal antigenicity were found by sequencing the glycophorin A (GPA) gene. This study demonstrates the systematic classification of these alleles to major or minor variations
N H Packer et al.
Electrophoresis, 19(6), 981-988 (1998-06-25)
Two-dimensional (2-D) electrophoresis is the preferred method for separating the glycoforms of proteins. The isoforms usually present as 'trains' of spots in the first dimension and may also differ in molecular weight. The primary goal for analyzing the carbohydrate content

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