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In medicine these proteins are useful and are used as a mitogen to trigger T-lymphocyte cell division and to activate latent HIV-1 from human peripheral lymphocytes.In neuroscience, anterograde tracing is a research method that uses the protein product phytohaemagglutinin PHA-L as a molecular tracer that can be taken up by the cell and transported across the synapse into the next cell thereby ...
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 ...
Illustration showing influenza virus attaching to cell membrane via the surface protein hemagglutinin. Hemagglutinins (alternatively spelt haemagglutinin, from the Greek haima, 'blood' + Latin gluten, 'glue') are homotrimeric glycoproteins present on the protein capsids of viruses in the Paramyxoviridae and Orthomyxoviridae families.
In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the lectin purified from sea urchin ( Anthocidaris crassispina ) eggs, SUEL. This lectin exists as a disulfide -linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. [ 1 ]
Structure of mannose in its α-D mannopyranose form. Mannan is a polymer of mannose.. The lectin pathway or MBL pathway is a type of cascade reaction in the complement system, similar in structure to the classical complement pathway, [1] in that, after activation, it proceeds through the action of C4 and C2 to produce activated complement proteins further down the cascade.
Download as PDF; Printable version; In other projects ... Pages in category "Lectins" ... Lectin-free diet; Lectin;
Collectin MBL is involved in activation of the lectin complement pathway. [32] [33] There are three serine proteases, MASP-1, 2 and 3 (MBL-associated serine proteases), which participate in activation of the lectin pathway. MASP-2 has a cleavage activity and it is essential for forming lectin C3 and C5 convertases and for activation of the ...
All three known members of the selectin family (L-, E-, and P-selectin) share a similar cassette structure: an N-terminal, calcium-dependent lectin domain, an epidermal growth factor (EGF)-like domain, a variable number of consensus repeat units (2, 6, and 9 for L-, E-, and P-selectin, respectively), a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto).