Anti-Fibulin-1 Antibody, clone 3D12.1 C화학적 특성, 용도, 생산
용도
Research Category Cell Structure
일반 설명
Fibulin-1 (UniProt P23142; also known as FIBL-1) is encoded by the FBLN1 (also known as FIBL1, FBLN, PP213) gene (Gene ID 2192) in human. Fibulin-1 is an extracellular matrix protein that interacts with fibronectin and inhibits cell migration and invasion in a fibronectin-dependent manner. Research shows that the EGF-like domains 5 and 6 of fibulin-1 compete against syndecan-4 for binding the C-terminal heparin-binding domain (HepII) of fibronectin, resulting in a suppression of fibronectin-regulated cell adhesion and motility. Fibulin-1 also interacts with fibrinogen and regulates platelet adhesion to influence hemoglutination. In addition, fibulin-1 interacts with elastin and plays a role in the assembly of elastic fibers by mediating association between versican and fibrillin. Other fibulin-1 interactors include calumenin, extracellular matrix protein 1, angiogenin, and hemicentin. There exist four major fibulin-1 isoforms (A, B, C, and D) generated by alternative splicing, with isoforms C and D being the predominant forms. In addition, a smaller isoform of fibulin-1D, fibulin-1D′, is reported to localize in the cytosol and interacts with the intracellular domain of integrin β1. Fibulin-1 is initially produced with a signal peptide (a.a. 1-29), the removal of which yields the mature protein with three N-terminal Anaphylatoxin-like domains (a.a. 36-76, 77-111, 112-144), followed by eight EGF-like domains (a.a. 176-578 of isoform D), with EGF-like domains 5 & 6 mediating fibulin-1 self-association and fibronectin-binding. The C-terminal 137-amino acid in isoform D is truncated in isoform A, and replaced by a shorter sequence of 35 amino acids in isoform B and a sequence of 117 amino acids in isoform C.
