Multimerin-1, also known as MMRN1, EMILIN-4 or ECM (endothelial cell multimerin), is a 1,228 amino acid secreted protein that contains one C1q domain, one EMI domain and one EGF-like domain. Synthesized in megakaryocytes and endothelial cells and present in liver, lung and placenta, Multimerin-1 exists as a multimeric structure composed of varying disulfide-linked multimers and functions as a carrier protein for platelet factors (specifically platelet factor V), playing a role in the stabilization and storage of factor V in platelets. In addition, Multimerin-1 acts as a ligand for select Integrins and may participate in extracellular matrix adhesion. Defects in the gene encoding Multimerin-1 that lead to Multimerin-1 deficiency are associated with autosomal dominant bleeding disorders due to platelet factor malfunction. Multiple isoforms of Multimerin-1 exist due to alternative splicing events.
155 kDa platelet multimerin; Elastin microfibril interface located protein 4; Elastin microfibril interfacer 4; EMILIN-4; Endothelial cell multimerin; glycoprotein Ia*; Multimerin-1; p-155; p155; Platelet glycoprotein Ia*
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