Human Contactin-2/TAG1 Alexa Fluor® 700-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Contactin-2/TAG1

Contactin-2 (CNTN2), also called TAG-1 (transient axonal glycoprotein), TAX1 (transiently-expressed axonal glycoprotein), or axonin-1, is a 135 kDa glycosyl‑phosphatidylinositol (GPI)- anchored cell adhesion molecule that belongs to the contactin subfamily within the immunoglobulin (Ig) protein superfamily (1‑3). Human Contactin-2 cDNA encodes a 28 amino acid (aa) signal peptide, a 984 aa mature secreted protein with six Ig-like domains followed by four fibronectin type III‑like repeats, and a 28 aa C-terminal GPI anchor pro-sequence. GPI-specific phospholipase activity can release soluble, active Contactin-2 from the membrane (2). Mature human Contactin-2 shares approximately 93%, 93% and 75% aa sequence identity with human, rat and chicken Contactin-2, respectively. During development, Contactin-2 is expressed by a subset of neuronal populations in the central nervous system (CNS) and peripheral nervous system (PNS), particularly during initial phases of axon outgrowth (3‑5). Both the 135 kDa form and a 90 kDa form are also upregulated in response to CNS injury in the adult (6). Data support a role for Contactin-2 in axon pathfinding, neurite outgrowth and adhesion, especially in the CNS (36). In mature myelinated fibers, Contactin-2 is expressed by oligodendrocytes and Schwann cells, which are myelinating glial cells of the CNS and PNS, respectively (7, 8). It is enriched in the juxtaparanodal regions, where it recruits caspr2 (Contactin-associated protein 2), a transmembrane neurexin involved in cell adhesion and intercellular communication (7‑10). The axonal Contactin-2 interacts in cis with caspr2, and in trans with another Contactin-2 on the glial membrane (8). This ternary complex is required for the accumulation and organization of K⁺ channels in the juxtaparanodes (9).

Product Datasheets

Related Research Areas

• Contactins
• Immunoglobulin Superfamily CAMs
• Synaptic Adhesion Molecules