Recombinant Human MDGA1 Protein, CF

MDGA1 (MAM domain containing glycosylphosphatidylinositol anchor 1) is a 135‑140 kDa glycoprotein within the IgCAM superfamily of adhesion molecules (1‑3). MDGA1 is thought to mediate neuronal migration, neurite outgrowth, and cell-cell adhesion within the central and peripheral nervous system (1, 4‑8). Human MDGA1 precursor is a 955 amino acid (aa) protein that produces a 914 aa mature protein with six Ig-like domains, a fibronectin type III domain (aa 640-739), a MAM domain (aa 751-918), and a GPI anchor (aa 932) (1-3). Mature human MDGA1 shares 95%, 96%, and 98% aa sequence identity with mature mouse, rat, and canine MDGA1, respectively. Potential human variants of 973, 904 and 587 aa contain a 48 aa substitution for aa 936-955, a 58 aa substitution for aa 847-955, and a 51 aa substitution for aa 537-955, respectively. Human MDGA1 also shares 54% aa sequence identity with human MDGA2, and may also share some functional redundancy (1, 4). MDGA1 is mainly expressed on restricted populations of neurons in the central and peripheral nervous system, such as embryonic neurons destined for cortical layers 2/3, migrating basilar pontine neurons and D1 interneurons of the spinal cord (1, 5‑7). Deletion or down‑regulation of mouse MDGA1 slows radial migration of neurons, indicating a role for MDGA1 in radial migration of cortical neurons (4, 5). MAM and Ig-like domains are involved in heterophilic and homophilic adhesion (7, 8). MDGA1 expression is also reported on primary cells and cell lines from leukemias, lymphomas, and tumors of the lung, colon, uterus, stomach and breast (3).