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Stillmark isolated ricin, an extremely toxic hemagglutinin, from seeds of the castor plant (Ricinus communis). The first lectin to be purified on a large scale and available on a commercial basis was concanavalin A, which is now the most-used lectin for characterization and purification of sugar-containing molecules and cellular structures. [36]
Phytohaemagglutinin (PHA, or phytohemagglutinin) is a lectin found in plants, especially certain legumes. PHA actually consists of two closely related proteins, called leucoagglutinin (PHA-L) and PHA-E. These proteins cause blood cells to clump together. PHA-E cause erythrocytes (red blood cells) to clump.
Influenza hemagglutinin: a homotrimeric glycoprotein that is found on the surface of influenza viruses which is responsible for their infectivity. [13] Influenza strains are named for the specific hemagglutinin variant they produce, along with the specific variant of another surface protein, neuraminidase.
In molecular biology, the leguminous lectin family is a family of lectin proteins. It is one of the largest lectin families with more than 70 lectins reported in a review in 1990. [ 1 ] Leguminous lectins consist of two or four subunits , each containing one carbohydrate-binding site.
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23845 Ensembl ENSG00000258227 ENSMUSG00000029915 UniProt Q9NY25 Q9R007 RefSeq (mRNA) NM_001301167 NM_013252 NM_001038604 NM_021364 RefSeq (protein) NP_001288096 NP_037384 NP_001033693 NP_067339 Location (UCSC) Chr 7: 141.93 – 141.95 Mb Chr 6: 40.55 – 40.56 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse C-type lectin domain family 5 member A (CLEC5A), also known as C-type lectin ...
A C-type lectin (CLEC) is a type of carbohydrate-binding protein known as a lectin. [3] The C-type designation is from their requirement for calcium for binding. [ 4 ] Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis .
In molecular biology, the haemagglutination activity domain is a conserved protein domain found near the N terminus of a number of large, repetitive bacterial proteins, including many proteins of over 2500 amino acids.