|Detection of Human FERMT3 by Western Blot. Western blot shows lysates of human platelets. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human FERMT3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7004) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for FERMT3 at approximately 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
FERMT3 (Fermitin family homolog 3; also kindling-3, MIG2B and URP2) is a 72-78 kDa member of the kindling family of proteins. It is a cytoplasmic protein that is expressed by B cells, T cells, platelets, neutrophils and vascular endothelial cells. FERMT3 acts on the cytoplasmic tails of beta -integrins 1 thru 3 to induce a conformational change and activation. This allows for expressing cell adhesion and arrest. Human FERMT3 is 667 amino acids (aa) in length. It contains a poly-Lys region (aa 147-155) plus a FERM domain (aa 229-558) that itself possesses a membrane-anchoring Pleckstrin homology domain (aa 354-457). There are three utilized phosphorylation sites at Ser8, Tyr11 and Tyr504. There are also two splice variants. One is 56 kDa in size and represents the use of an alternative start site at Met181, while a second contains a deletion of aa 360-363. Over aa 498-667, human FERMT3 shares 99% aa identity with mouse FERMT3.
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